Amytracker

Amytracker are small fluorescent molecules for detection of protein aggregates suitable for use in fibrillation assays, fixed or fresh tissue sections and cells as well as systemic injection in vivo. They are exceptionally photo- and thermostable and allow for easy handling in any application. Amytracker work in a wide range of salt and pH conditions. When the pH is altered during the experiment, pH controls should be included.

Amytracker can be used with fluorescence plate readers, fluorescence microscopes and confocal laser scanning microscopes, fluorescence life time imaging (FLIM), fluorescence cytometry (FACS), Total internal reflection fluorescence (TIRF) microscopy and Multiphoton microscopy

Five Amytracker variants are available specified by their peak emission wavelength. All Amytracker variants are designed to bind to the Congo red binding pocket on the amyloid fibril. A minimum of eight in-register parallel-β-strands are required for binding. The Amytracker variants differ in affinity and spectral properties. As Amytracker are structural markers, you can achieve reliable fluorescent labeling of amyloids derived from a variety of amyloidogenic proteins or peptides from different species.

You can choose between four different formulations. 

  • Aqueous: 1 mg/ml solution in ultrapure water. The product should be diluted 1:1000 before use. For use in live-cells, sometimes 1:500 is necessary due to uptake limitations. To prevent evaporation of the aqueous solvent, close the container carefully after use, spin down liquid and use up small volumes quickly.
  • DMSO: 1 mg/ml solution in DMSO to prevent solvent evaporation. The product should be diluted 1:1000 before use. For use in live-cells, sometimes 1:500 is necessary due to uptake limitations
  • Solid: 1 mg solid lyophilised in a sterile injection bottle. We recommend dilution to 4 mg/ml in physiological saline followed by intravenous injection with a total dose of 5 mg/KG
  • Drop&Shine: 5 ml ready-to-use product in mounting medium. Ideal for use in tissue sections. Add a some Drop&Shine and mount your slide to detect amyloids within minutes.

Store your Amytracker product in the fridge and use the opened container within 12 months. Amytracker is for research use only and is not for resale.

Amytracker visualizes Aβ aggregates in Alzheimer’s organoid models
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Amytracker visualizes Aβ aggregates in Alzheimer’s organoid models

Brain organoids are self-assembled three-dimensional aggregates generated from pluripotent stem cells. They offer a reproducible, optimized platform filling in the gap that traditional models for neurodegenerative diseases struggle to address. In a recent study from The Scripps Research Institute, Sergio R. Labra and colleagues developed an advanced human cerebrocortical organoid (CO) model to investigate early events in familial Alzheimer’s disease (AD). Using human iPSCs, the team generated organoids carrying heterozygous mutations in key AD-associated genes, PSEN1 (PSEN1ΔE9/WT, PSEN1M146V/WT) or APP (APPSwe/WT), and compared them to isogenic wild-type controls (WT/WT). The COs were extensively characterized using immunohistochemistry, single-cell RNA sequencing, electrophysiology,... Read more →
Amytracker for staining recombinant Spider Silk microspheres
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Amytracker for staining recombinant Spider Silk microspheres

Biomaterials composed of self-assembling protein building blocks are being actively explored for biomedical applications, including drug delivery, tissue engineering scaffolds, and functionalized surface coatings. Among these, spider silk has attracted particular attention due to its biocompatibility and stability. However, large-scale production of natural spider silk remains challenging, which has led to the development of recombinant spider silk proteins such as FN-silk (FN-4RepCT), functionalized with a cell-binding motif (RGD). FN-silk has previously been shown to form fibrillar structures at air-liquid interfaces, and more recently, to self-assemble into microspheres within physiological buffer (PBS) solutions. In this study, Ornithopoulou et al. (2023) used... Read more →
Tracing Tau: A Step Closer to Understanding Neurodegeneration
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Tracing Tau: A Step Closer to Understanding Neurodegeneration

Tauopathies, including Alzheimer's disease (AD) and Pick’s disease, are characterized by the aggregation of tau proteins into insoluble filaments. Traditional cell-based assays modelling tau seeding often rely on mutant or truncated tau, limiting their relevance to sporadic tauopathies. In a study published in the Journal of Biological Chemistry, Huang and McEwan developed a biosensor assay based on HEK293 cell lines stably over-expressing full-length, wild-type tau isoforms to more accurately model disease conditions. They demonstrated that wild-type tau, without disease-associated mutations, is sufficient to develop sensitive and disease-relevant seeding assays when using brain-derived tau aggregates. Moreover, they showed that the aggregates... Read more →
Finding the Invisible: How Amyloid Detection Is Improving
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Finding the Invisible: How Amyloid Detection Is Improving

Neurodegenerative diseases, such as Parkinson’s, often begin decades before clinical symptoms are observed. Early detection is crucial, but identifying disease biomarkers - like the low concentrations of α-synuclein aggregates - is incredibly challenging. In a study published in Angewandte Chemie, Azad Farzadfard and colleagues explore how to facilitate the detection of small amounts of these aggregates in biological samples. They achieved higher sensitivity by modifying the prion disease seed aggregation assay into a more sensitive microemulsion seed aggregation assay (SAA). By using Amytracker, the researchers confirmed that under fully quiescent conditions, α-synuclein amyloid fibril amplification was suppressed in the microemulsion... Read more →
Glycosylation guides a safer strain of α-synuclein
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Glycosylation guides a safer strain of α-synuclein

Aggregated α-synuclein is part of the pathology of Parkinson’s disease and dementia with Lewy bodies, but why these oligomeres and fibrils aggregate as part of these diseases - or how to stop it - is unknown. In a study published in Nature Chemical Biology, Aaron Balana and colleagues investigated the effects of the post-translational modification O-GlcNAc (an intracellular form of glycosylation) of α-synuclein monomers. Using advanced structural tools such as cryogenic electron microscopy, they demonstrate that O-GlcNAcylation makes α-synuclein adopt a distinct fibril structure that reduces its seeding capacity - suggesting that it is less pathological. They found that this... Read more →
ApoE Aggregates and Innate Immunity: Insights into Endotoxin Sequestration
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ApoE Aggregates and Innate Immunity: Insights into Endotoxin Sequestration

Apolipoprotein E (ApoE) is widely recognized as a key genetic risk factor for Alzheimer’s disease.It is also implicated in other protein aggregation disorders such as Parkinson’s disease and Lewy Body dementia. Humans express three main alleles of the APOE gene, each associated with different levels of disease risk - APOE4, for instance, increases the risk of Alzheimer’s diseases by up to 15-fold in homozygotes, whereas APOE2 has a protective effect. Although the primary physiological function of ApoE is to mediate lipid transport and cholesterol metabolism throughout the body, it is also prone to aggregation and suggested to seed amyloid-β plaques.... Read more →
When Amyloids Meet Viruses: α-Synuclein Fibrils Enhance HIV-1 Infection
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When Amyloids Meet Viruses: α-Synuclein Fibrils Enhance HIV-1 Infection

HIV-associated neurocognitive disorders are observed in 30-50% of infected individuals, but they are poorly understood. A recent study published in Nature Communications uncovers a striking interaction between neurodegenerative disease-associated amyloids and HIV-1 infection. The group led by Frank Kirchhoff at Ulm Medical Center in Germany were able to visualize and confirm the presence of fibrillar α-synuclein and amyloid-beta (Aβ) in human cell lines, including T-cells and microglia. Using Amytracker 540 they revealed that these fibrils localize at the interface between virus and host cell, showing that they significantly enhance HIV-1 entry and replication in human cells. Amytracker made it possible... Read more →
Antibodies Against a Synthetic Aβ Trimer-Mimic to Map Amyloid Pathology
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Antibodies Against a Synthetic Aβ Trimer-Mimic to Map Amyloid Pathology

Understanding how amyloid-beta (Aβ) aggregates in Alzheimer’s disease (AD) is crucial for advancing diagnostics and treatment. Adam Kreutzer and their colleagues at the University of California Irvine developed a structurally defined Aβ trimer mimic, designed to resemble natural Aβ oligomers found in the brain. Using this trimer as an immunogen, they generated a polyclonal antibody that specifically recognizes early Aβ aggregates. With a combined staining of antibodies and Amytracker 680, the authors characterized different stages of Aβ aggregation and their distribution in brain of a mouse models of Alzheimer’s disease (5xFAD) as well as tissue from patients with Alzheimer’s disease... Read more →
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Unraveling Tau Propagation: Amytracker Reveals Astrocytic Pathways

Video: Astrocyte-to-astrocyte transfer of AD tau fibrils through tunneling nanotubes (TNTs). Time-lapse microscopy of Amytracker-labelled AD tau fibrils (shown in red) demonstrating direct cell-to-cell transmission between human astrocytes. Video from Online Resource 10 of Eltom, K., Mothes, T., Libard, S. et al. (2024) acta neuropathol commun (CC-BY-4.0) Tauopathies are a group of neurodegenerative diseases characterized by the accumulation of neurofibrillary tangles - hyperphosphorylated, insoluble aggregates of the microtubule-associated protein Tau. Although astrocytes, the brain’s most abundant cell type, are well known for their roles in synaptic function, tissues homeostasis, and neuroinflammation, their contribution to tauopathies remains only partially understood. Recent... Read more →
Copper’s role in prion protein misbehaviour
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Copper’s role in prion protein misbehaviour

Prion diseases are fatal neurodegenerative disorders caused by the misfolding and aggregation of prion proteins (PrP). Although copper (Cu2+) imbalance has long been suspected to play a role in these conditions, a recent study by Juliani and colleagues at the Federal University of Rio de Janeiro sheds new light on this issue. Their researchreveals that Cu2+ promotes the formation of liquid-like PrP condensates that naturally buffer excess copper and help prevent toxicity. However, under oxidative stress, these condensates transition from a liquid to solid state, forming amyloid-like aggregates that may contribute to disease progression. These findings suggest a critical link... Read more →
How functional amyloids help regulate stress responses
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How functional amyloids help regulate stress responses

Protein aggregation is traditionally seen as a pathological process, hallmark of neurodegenerative diseases and systemic amyloidoses. However, emerging evidence reveals that amyloid aggregation is not merely the consequence of protein misfolding; rather, cells harness reversible amyloid aggregation to adapt to environmental stress. Understanding how functional amyloids form and disassemble could provide critical insights into the treatment of pathological aggregation. The team led by Timothy Audas at Simon Fraser University, has recently published its work on Amyloid bodies (A-bodies) - nuclear amyloid-like inclusions that sequester proteins in response to environmental stressors. Similar to other stress-related inclusion (e.g. cytoplasmic stress granules) the... Read more →
Amytracker aids in designing small molecules to inhibit aggregation of α-synuclein
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Amytracker aids in designing small molecules to inhibit aggregation of α-synuclein

Small molecules with the ability to inhibit the nucleation process and stop the aggregation of α-synuclein have immense potential to help people suffering from Parkinson's. Availability of several aSyn protein structures has now opened the possibility to develop structure-based drugs that can specifically bind to and prevent α-synuclein aggregation. In a study, published in Molecular Pharmaceutics, researchers from the Centre for Misfolding Diseases at University of Cambridge aimed to identify such small molecules by using a structure-based drug discovery approach. First, they performed structure-based in-silico screening of small molecules that can bind to the aSyn and later experimentally verified the... Read more →
Oxidative stress and amyloid formation contributes to phenylketonuria disease
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Oxidative stress and amyloid formation contributes to phenylketonuria disease

Phenylketonuria is an inherited disorder characterised by the inability to break down the amino acid L-phenylalanine (L-Phe). The disease is primarily caused by mutations in the gene that encodes phenylalanine hydroxylase and there are >1000 human described variants, but the R261Q mutation is one of the most common mutations. A team of researchers from Norway and Switzerland used a mouse model with the desired R261Q mutation to study the effect of this mutation and the molecular basis of Phenylketonuria. In their study, Aubi et al. found that the male R261Q mice had higher body weight compared to the female cohort... Read more →
The structural basis of TDP-43 aggregation
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The structural basis of TDP-43 aggregation

Neurodegenerative diseases often involve the accumulation of misfolded proteins, that cells fail to refold or degrade and that eventually form aggregates. Among these, oligomers, which are small, still-soluble aggregates, are considered the most toxic and can lead to neuronal death. Identifying the aggregation-prone regions of these oligomer forming proteins is key for developing new therapeutic approaches. In over 97% of amyotrophic lateral sclerosis (ALS) cases, TDP-43 (TAR DNA/RNA-binding protein 43) condensates accumulate in the cytoplasm. The carboxy-terminal region of TDP-43 is processed into smaller aggregation-prone fragments that are included into these condensates. Akira Kitamura and their colleagues at Hokkaido University... Read more →
Uncovering a new link to amyloid formation in neurodegenerative diseases
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Uncovering a new link to amyloid formation in neurodegenerative diseases

The 14-3-3 proteins regulate various cellular functions, including enzymatic activity and protein stability. The 14-3-3ζ isoform has been linked to neurodegenerative diseases due to its interaction with proteins like tau and α-synuclein, which form amyloid fibrils in Alzheimer’s and Parkinson’s. However, its direct role in amyloid plaque formation remains unclear. A group of researchers from the Institute of Biotechnology in Vilnius aimed to determine if 14-3-3ζ can form amyloid fibrils. Using bioinformatic tools, they identified several aggregation-prone regions. To test amyloid formation under physiological conditions, they incubated 14-3-3ζ and monitored the process using amyloid-specific dyes: Thioflavin T, Congo Red, and... Read more →
Modular protein hydrogels for flexible applications
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Modular protein hydrogels for flexible applications

Hydrogels can be used as a 3D scaffold for cells to grow in tissue models and biofabrication applications. Such hydrogels can be made from proteins that form amyloid fibrils. Different biological applications have distinct requirements for the properties of these hydrogels. Designing a unique biopolymer for each application is cumbersome and to be able to assemble tailored systems from a set of predefined building blocks is beneficial. In a study, published in Acta Biomaterialia, researchers from ETH Zurich in Switzerland present an approach for a modular protein hydrogel platform. Their system allows the differentiation of hMSCs into osteoblasts, and the... Read more →
Amyloid formation in ALS: Redefining the role of TDP-43 inclusions
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Amyloid formation in ALS: Redefining the role of TDP-43 inclusions

Researchers from the University of Florence investigated the nature of TAR DNA-binding protein 43 (TDP-43) cytoplasmic inclusions, which are key pathological markers in neurodegenerative diseases like amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD). The study focused on whether these inclusions exhibit amyloid-like characteristics, as there has been debate over their structure and classification. The researchers conducted in situ and in vitro experiments to study TDP-43 inclusions. They expressed human TDP-43 in a motor neuron cell model and used Raman spectroscopy, FTIR, and TEM to examine aggregate structures. Purified TDP-43 was tested for amyloid formation using Amytracker 630. The... Read more →
Amytracker confirms amyloid nature of inclusion bodies in muscle linked to gene mutations
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Amytracker confirms amyloid nature of inclusion bodies in muscle linked to gene mutations

Distal myopathies are genetically heterogeneous diseases that primarily affect skeletal muscles, particularly in the hands and feet, although they can progress to other muscles. Previous research has identified more than 25 genes associated with these conditions, but many patients still remain undiagnosed. SMPX (small muscle protein X-linked), a gene involved in muscle function, has previously been associated with non-muscle-related conditions such as hearing loss, but a study from Folkhälsan Research Center in Finland reveals its role in distal myopathy with protein inclusions. The study, published in Acta Neuropathologica performed deep phenotyping and genetic sequencing on 10 patients from 9 families,... Read more →
Estrogen might be women’s secret weapon!
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Estrogen might be women’s secret weapon!

Alzheimer's disease (AD) affects women more than men. However, we don’t really know why. Women tend to live longer, which may contribute to a higher incidence of AD, but other factors, such as hormonal changes during menopause, could also influence disease progression. In a study, published in Translational Psychiatry, researchers from the Centre for Brain Research in Bangalore explored why females exhibit a delayed onset of AD-related cognitive impairments how hormonal changes impact this progression. The researchers used male and female APP/PS1 transgenic mice which present with an AD phenotype relatively early in life to examine how synaptic protein translation... Read more →
Transition to aggregation in hnRNPA1A condensates visualised using Amytracker
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Transition to aggregation in hnRNPA1A condensates visualised using Amytracker

Amyotrophic lateral sclerosis (ALS) and frontotemporal dementia are associated with the aggregation of certain RNA-binding proteins that are part of stress granules, including TAR DNA-binding protein 43 (TDP-43), Fused in Sarcoma (FUS) and Heterogeneous nuclear ribonucleoprotein A (hnRNPA). Stress granules are cytoplasmic membraneless organelles that are formed in response to stresses that halt protein production. These organelles collect the mRNA that was being translated, possibly to protect the RNA or to ensure that no damaged proteins are produced. A study by Morelli et al. published in Nature Chemistry investigates how interactions with RNA modulate the aggregation of hnRNPA1A. Using an... Read more →
Amytracker shows how α-Synuclein aggregates at the mitochondrial membrane
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Amytracker shows how α-Synuclein aggregates at the mitochondrial membrane

Faulty α-synuclein (α-Syn) aggregates in cells forming toxic α-Syn oligomers and finally Lewy Bodies which are the pathological hallmark of synucleinopathies. While Lewy Bodies are relatively easy to discern in a microscope, it turns out to be very difficult to investigate the early-intermediate forms of aggregates. A study published in the journal Nature Neuroscience presents an assay to gain insight on the early events of α-Syn aggregation. In their paper Choi et al. make use of a phenomenon called Förster resonance energy transfer (FRET) which can assess to detect if light sensitive molecules are in very close contact to each... Read more →
Studying the relationship between morphology and inflammatory effect of ɑ-synuclein aggregates
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Studying the relationship between morphology and inflammatory effect of ɑ-synuclein aggregates

Parkinson's disease (PD) and Multiple System Atrophy (MSA) are both characterized by accumulation and misfolding of ɑ-synuclein (ɑ-syn). However, there are distinct differences between their pathology likely relating back to different strains of ɑ-syn aggregates. The goal of a study by De Luca et al. from IRCCS and SISSA in Italy was to analyze how neuronal SH-SY5Y cells reacted to different forms of ɑ-syn aggregates isolated from the olfactory mucosa of patients with PD and MSA as well as healthy controls using a Seed Amplification Assay. While ɑ-syn isolates from PD and MSA patients showed an efficient seeding activity, those... Read more →
Faulty ribosome quality control triggers amyloid aggregation
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Faulty ribosome quality control triggers amyloid aggregation

What causes the accumulation of toxic amyloid aggregates? An article by the group of Bingwei Lu from the Department of Pathology at Stanford University School of Medicine published in the journal Acta Neuropathologica Communications might have found the answer to this question. Their work shows that a defective ribosome quality control (RQC) causes the C-terminal fragment (APP.C99) of the Amyloid precursor protein (APP) to accumulate. This might be one of the earliest pathogenic events of amyloid aggregation. Labelling such aggregates in HeLa cells with Amytracker 680 shows that they have amyloid-like properties. Image: Ribosome stall-induced APP.C99 with C-terminal extensions seeds... Read more →
Amytracker labels amyloid forms of tau in a cell based model for tauopathies
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Amytracker labels amyloid forms of tau in a cell based model for tauopathies

Accumulation of abnormal tau protein in the brain has been described as pathological hallmark of a group of neurodegenerative disorders called tauopathies. The most common tauopathy is Alzheimer’s disease (AD). In AD, intracellular inclusions containing aggregates of hyperphosphorylated tau coexist with extracellular amyloid plaques containing aggregated amyloid-β (Aβ). Clinically, tau inclusions correlate with cognitive impairment and therefore tau pathology is considered to be the major driver for neuronal degeneration and has become a target of rapidly evolving therapeutic strategies. Tau plays an important physiological function in dynamically interacting with axonal microtubules and is the target of various post-translational modifications. It... Read more →
Amyloids trigger proinflammatory signalling Multiple Myeloma
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Amyloids trigger proinflammatory signalling Multiple Myeloma

Multiple myeloma is a complex B-cell malignancy characterised by the accumulation of malignant plasma cells. Progression of multiple myeloma is related to dysregulated inflammatiory processes; especially leucocytes and tumor-associated macrophages (TAMs) are central during the initiation and progression of the disease and high concentration of TAMs often relates to drug resistance and fast proliferation. TAMs produce proinflammatory cytokines whose production is controlled carefully in the cell under normal circumstances. The production and release of proinflammatory cytokines is controlled by nod-like receptor NLRP3. While the activation process of NLRP3 is poorly understood, it has been found that, among other triggers, endogenous... Read more →
Amytracker: a tool to identify toxic dipeptide repeats
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Amytracker: a tool to identify toxic dipeptide repeats

Repetitive genomic regions are known to expand across generations, due to errors during their replication, and cause a series of - mainly - neurological diseases collectively called repeat expansion diseases. One of these repetitive genomic regions is the GGGGCC (G4C2) locus in the C9orf72 gene. Its expansion is linked with amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD). It is still unclear, however, whether the cytotoxic effects of the repeat-expansion are emerging from the G4C2 mRNA, or from the results of its translation. Frederic Frottin from F. Ulrich Hartl’s group at the Max Planck Institute of Biochemistry and Mark S... Read more →
How mutations contribute to pathological diversity in synucleopathies
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How mutations contribute to pathological diversity in synucleopathies

Alpha-synuclein (α-Syn) is a presynaptic neuronal protein encoded by the SNCA gene. It is expressed heavily in the brain and regulates synaptic vesicle trafficking and subsequent neurotransmitter release. Under certain conditions, α-Syn aggregates and forms, together with other components, intracellular inclusions called Lewy bodies (LBs) or Lewy Neurites (LN), which are the defining pathological hallmark of many synucleinopathies. Several familial mutations of the SNCA gene have been identified causing LB and LN pathology, but manifest in different diseases like Parkinson's Disease, Dementia with Lewy bodies (DLB) or Multiple System Atrophy (MSA), suggesting that the various mutations may act via distinct... Read more →
Deciphering the complexity of intracellular Tau aggregates
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Deciphering the complexity of intracellular Tau aggregates

Tau is an intrinsically disordered protein with the key function to stabilise axonal microtubules. In several neurological disorders collectively known as Tauopathies, tau proteins form aggregates that accumulate in cells and cause neuronal damage. The molecular mechanism which leads to tau aggregation is complex and liquid–liquid phase separation (LLPS), a process that is used by cells to assemble membrane‐less organelles, has been found to be involved in Tau aggregation. De-mixing of Tau can be triggered through the addition of macromolecular crowding agents, or through coacervation (i.e. co-condensation of the positively charged Tau microtubule‐assembly domain with polyanionic RNA into liquid‐like droplets).... Read more →
Linking aggregate size and toxicity using Amytracker
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Linking aggregate size and toxicity using Amytracker

In the context of neurodegenerative diseases, large, fibrillar amyloid deposits - such as Lewy bodies, Amyloid plaques, and Neurofibrillary tangles - characterize the pathology of the disease but it has recently become evident that small, spherical aggregates below 20 nm in diameter are mainly responsible of the toxic response that results in neurodegeneration. The small size of these aggregates makes their detection difficult, especially within biologically relevant environments. To tackle this issue, Michael Morten and their colleagues at the Imperial College in London have developed a method for single-molecule localization microscopy (SMLM) using aggregate-activated fluorophores. Initially, they benchmarked Alexa647, Thioflavin... Read more →
Protein aggregation in wound healing
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Protein aggregation in wound healing

Lipopolysaccharide (LPS) is a cell envelope glycolipid produced by most gram-negative bacteria. When LPS is recognized by Toll-like receptor 4 (TLR4) an innate host-response to bacterial infection is triggered. To achieve a robust antibacterial response while maintaining control of inflammatory processes, LPS has to be cleared from the infection site. A group of researchers around Prof. Artur Schmidtchen from the Division of Dermatology and Venereology at Lund University have investigate the mechanism of LPS clearing from wounds and shown that addition of LPS or bacteria to acute wound fluid (AWF) leads to precipitation of proteins mediating LPS aggregation and scavenging.... Read more →
Phase separated α-synuclein is more prone to aggregation
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Phase separated α-synuclein is more prone to aggregation

Alpha-synuclein (α-Syn) aggregation hallmarks a group of neurodegenerative diseases known as synucleinopathies with Parkinson’s disease as its most well-known representative. The molecular mechanism behind the aggregation of α-Syn is still not completely understood. Many aggregation-prone proteins, like α-Syn, are known to form phase-separated condensates and recent findings suggest that the early events that lead to protein aggregation, amyloid deposition, and ultimately neurodegeneration, are happening within these condensates. Recent work from Piroska et al. published in the journal Science Advances found strong evidence of a connection between phase separation and aggregation of α-Syn. When α-Syn was present in form of a... Read more →
FL-OPTIR for studying biophysical properties of amyloids in cells and tissues
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FL-OPTIR for studying biophysical properties of amyloids in cells and tissues

Infrared (IR) spectroscopy is an invaluable tool to study the biophysical properties of amyloid aggregates. Although historically used as a tool for composition analysis of chemical compounds as it measures the vibrational energy of chemical bonds, IR spectroscopy provides measures to analyse the size and rigidity of amyloid fibrils. Coupling of IR spectroscopy to an optical microscope (OPTIR) is a new method that allows users to obtain chemical information of biological macromolecules from cells and tissues at submicron resolution. Using OPTIR for investigating the biophysical properties of amyloid fibrils in cells and tissues has been challenging since amyloid fibrils cannot... Read more →
Spatial pattern of microglial activation in relation to amyloid plaques
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Spatial pattern of microglial activation in relation to amyloid plaques

Microglia cells play a vital role in regulating brain development, maintenance of neuronal networks, and injury repair. Their involvement in the progression of protein aggregation leading to neurodegenerative diseases is complex. While they can clear amyloid plaques and prevent their accumulation, dysfunctional microglia regulation may be a key factor in disease progression. Microglia can “sense” accumulation of amyloid plaques which leads to a change in the expression patterns of Plaque Induced Genes (PIGs). One well-known PIG is Trem2, a microglial membrane receptor protein linked with Alzheimer’s disease (AD). A key function of Trem2 is to induce the microglia cells towards... Read more →
Amyloidogenicity of SARS-CoV-2 spike protein
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Amyloidogenicity of SARS-CoV-2 spike protein

Infection with SARS-CoV-2 leads to patients developing the COVID-19 disease, which is a complex hyperinflammatory syndrome, characterised by acute respiratory distress (ARD). Aside from these severe respiratory symptoms, we now know that the virus can present in unexpected, varied, and long-lasting manners. Recent studies hint towards the amyloidogenicity of the SARS-CoV-2 spike protein (Nyström, S. et al. 2022) and indicate the presence of amyloid aggregates in plasma clots from patients suffering from Long-Covid symptoms (Pretorius, E. et al. 2021) Researchers from the University of Lund in Sweden and the National University of Singapore previously found that spike protein binds to... Read more →
Lewy body formation in seeding based neuronal models
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Lewy body formation in seeding based neuronal models

Parkinson’s disease is a brain disorder that causes unintended or uncontrollable movements, such as shaking, stiffness, and difficulty with balance and coordination. Symptoms usually begin gradually and worsen over time. As the disease progresses, people may have difficulty walking and talking. The basis of these symptoms is progressive neurodegeneration and accumulation of degradation-resistant intracellular aggregates, termed Lewy bodies, throughout the brain. One of the major components of Lewy bodies is α-synuclein, a small protein that normally localizes at the presynaptic terminal of neurons where it regulates the release of neurotransmitters and possibly participates in the assembly of the cytoskeleton. The... Read more →
Prolonged stress leads to accumulation of misfolded proteins in the nucleolus
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Prolonged stress leads to accumulation of misfolded proteins in the nucleolus

The nuclear proteome is rich in proteins which are prone to aggregate upon conformational stress. This might explain why intranuclear inclusions can often be found in neurodegenerative disorders associated with protein aggregation. Using a combination of fluorescence imaging, biochemical analyses, and proteomics, researchers at Max Planck Institute for Biochemistry around Prof. F.-Ulrich Hartl have investigated the role of the nucleolus as a “phase-separated protein quality control compartment” and published their results in the renowned scientific journal Science. The nucleolus is the largest non–membrane-bound nuclear subcompartment and consists of liquid-like phases that do not intermix, giving rise to distinct zones. To... Read more →
Amytracker can be used for intracerebral multiphoton microscopy
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Amytracker can be used for intracerebral multiphoton microscopy

A team of researchers from Massachusetts General Hospital and Harvard Medical School as well as Linköping University have used a fluorescent probe of the same type as Amytracker for multiphoton imaging of Amyloid-β deposits in transgenic mice in vivo. The fluorescent molecule clearly targeted and labeled core plaques in the cerebral tissue and vasculature when imaged after intravenous injection. The fluorescent signal appeared already shortly after injection, however reaching maximal intensity between 24 and 72 hours – clearly showing the capacity of the probe to pass the blood brain barrier without causing toxicity. Since core plaques are labeled intensely with... Read more →
The clue to detect multiple systems atrophy?
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The clue to detect multiple systems atrophy?

In a study, recently published in Nature, a fluorescent tracer molecule similar to Amytracker has been used to detect α-synuclein aggregates in cerebrospinal fluid from patients with synucleopathy. Interestingly, the fluorescent tracer molecule was binding aggregates from patients with Multiple Systems Atrophy with higher affinity than aggregates from patients with Parkinson’s Disease. While aggregates of α-synuclein in distinct synucleinopathies have been proposed to represent different conformational strains of α-synuclein, this is the first study that provides distinct clues that can be used in future diagnostic assays. Read More: Shahnawaz M. et al. (2020) Discriminating α-Synuclein Strains in Parkinson’s Disease and... Read more →
Anomalous fibrin amyloid formation
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Anomalous fibrin amyloid formation

Lipopolysaccharides (LPS) from the Gram-negative cell envelope can be shed from dormant bacteria or from continual bacteria entry into the blood and serve to contribute to the chronic inflammation. The presence of highly substoichiometric amounts of LPS from Gram-negative bacteria caused fibrinogen clotting to lead to the formation of an amyloid form of fibrin. The teams around Prof. Douglas B. Kell from the University of Manchester and Prof. Etheresia Pretorius from the Stellenbosh University have shown that the broadly equivalent lipoteichoic acids (LTAs) from two species of Gram-positive bacteria have similarly (if not more) potent effects than LPS. Specifically they... Read more →
Amyloids in type-2 diabetes
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Amyloids in type-2 diabetes

Type-2 diabetes is a progressive condition marked by resistance towards the blood-sugar regulating hormone insulin. Recently, Type-2 diabetes is become recognized as an inflammatory condition which is often accompanied by cardiovascular complications. The teams around Prof. Etheresia Pretorius from Stellenbosh University and Prof. Douglas B. Kell from the University of Manchester investigated blood clot formation from plasma of diabetic patients. Using advanced confocal microscopy and Structured Illumination Superresolution Microscopy, the authors found that plasma clots from diabetic patients contain significant amounts of amyloid hinting towards an inflammatory cue for the occurrence of cardiovascular symptoms in Type-2 diabetes. Read More: Pretorius,... Read more →
Advanced imaging
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Advanced imaging

In a new study in the Journal of visualized experiments, the team around Prof. Peter Nilsson and Prof. Per Hammarström from Linköpings University describe how luminescent conjugated oligothiophenes (LCOs) can be used with Hyperspectral Imaging (HIS) and Fluorescence Lifetime Imaging (FLIM) to detect amyloid species. In a practical approach, the authors highlight caveats of LCO staining and give valuable advice on troubleshooting. Read More: Nyström et al. (2017) Imaging amyloid tissues stained with luminescent conjugated oligothiophenes by hyperspectral confocal microscopy and fluorescence lifetime imaging. Journal of Visualized Experiments, 2017(128) Read more →
Protein engineering for better PET radioligands
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Protein engineering for better PET radioligands

An approved method for visualization of Amyloid β (Aβ) plaques in patients suffering from Alzheimer's disease is Positron Emission Tomography (PET). This method requires a radiolabeled amyloid ligand. A frequently used molecule is Pittsburgh Compound B (PIB) which is a derivative of Thioflavin T. Radiolabeled PIB is well-suited to visualize insoluble Aβ plaques and has been used for differential diagnosis of AD. However, the PIB signal, giving an estimate of total plaque load becomes saturated early in the disease progression. To being able to diagnose Alzheimer's disease early-on, soluble forms of aggregated Aβ like oligomers and protofibrils need to be... Read more →
Artifical amyloids
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Artifical amyloids

A team of scientists around Frederic Rousseau from Switch Laboratory at KU Leuven have designed a biologically active amyloid from a peptide sequence occurring in vascular endothelial growth factor 2 (VEGFR2). The peptide, which the researchers named vascin forms artificial amyloids. The results show, however, that vascin amyloids are not inherently toxic but that the emergence of amyloid toxicity is dependent on the biological context. When vascin oligomers are applied to cultured cells, they are efficiently absorbed and lead to a functional knockdown of VEGFR2. As such, vascin oligomers are only toxic to cells that rely on VEGFR2 signalling. LCOs... Read more →
Testimonial - Shan Huang

Testimonial - Shan Huang

Shan Huang (Inscopix) about Amytracker 520 Solid "We’ve been using Amytracker 520 to label Aβ plaques in vivo in 5xFAD mice with our nVista miniscope, and it has performed exceptionally well. The dye provides strong, specific labeling of amyloid plaques with high signal-to-noise and minimal background, even under the constraints of 1-photon imaging. Amytracker 520 crosses the blood-brain barrier efficiently and enables longitudinal tracking of plaque progression in freely behaving animals." Shan Huang (PhD), Senior Research Scientist, Inscopix, Mountain View, CA, USA Amytracker 520-labeled plaques in 5xFAD mice imaged by Inscopix nVista miniscope system. Images were kindly provided by Shan... Read more →
Testimonial - Leon Smyth

Testimonial - Leon Smyth

Leon Smyth about Amytracker 520 Solid We have used AmyTracker-520 for tissue staining, pulse-chase experiments to define plaque growth, and intravital imaging and it is excellent for all these applications. It is particularly useful having a range of colors to choose from for compatibility with microscope filters and transgenic reporters for intravital applications. Leon Smyth, PhD, Postdoctoral Research Associate, Washington School of Medicine in St. Louis 2-Photon microscopy of AmyTracker-520 labelling in 6-month-old 5XFAD mouse brain. Labelling is present in parenchymal plaques and cerebral amyloid angiopathy. Orange = blood vessels labelled with IV dextran, green = AmyTracker-520. Image was kindly... Read more →
Testimonial - Linh Tran

Testimonial - Linh Tran

Linh Tran about Amytracker 480 and Amytracker 680 "I have the opportunity to work with Amytracker dyes for my PhD project and find them to be exceptional. These dyes deliver superb brightness and an excellent signal-to-noise ratio, making them an outstanding tool for the fluorescent visualization of amyloid-beta. On tissue sections, the staining procedure is both simple and quick. Amytracker dyes complement other amyloid probes that I use, offering promising potential for gaining additional insights into amyloid pathology. In addition, technical consultation with Ebba team was pleasant and efficient, making the entire process a great experience." Linh Tran, PhD student,... Read more →
Testimonial - Manuela Leri

Testimonial - Manuela Leri

Manuela Leri about Amytracker 630 "I used the Amytracker 630 probe to visualize intracellular aggregates on cell cultures. I obtained excellent results using confocal microscopy. The cells were permeabilized and the probe recognized the primary antibody used very well and emitted a good signal. The signal is stable." Manuela Leri (PhD) Postdoctoral Researcher, Department of Experimental and Clinical Biomedical Sciences, University of Florence, Italy SH-SY5Y neuroblastoma cells were treated with okadaic acid (LEFT) to induce hyperphosphorylation of Tau. Control cells (RIGHT) were left untreated. Amytracker 630 was used to label aggregates emerging in live cells. Images were kindly provided from... Read more →

Testimonial - Azad Farzadfard

Azad Farzadfard about Amytracker 580 and Amytracker 680 "Amytracker was a great substitute for ThT in visualizing the alpha-synuclein fibrils inside the water-in-oil emulsion droplets made in microfluidic devices. ThT leakage from these droplets was an issue that was resolved by Amytracker products. I started by using Amytracker 480 that was a great upgrade for my experiments in compare to ThT. No leakage and footprint on PDMS was observed, but Amytracker 480 still showed background inside the droplets in my setup. Replacing it with Amytracker 680, however, removed the background completely with high sensitivity for the fibrils." Azad Farzadfard (PhD)... Read more →
Testimonial - reMynd

Testimonial - reMynd

Tom Cornelissen, PhD, reMYND Science Director Contract Research: “At reMYND's Contract Research Organization (CRO), we specialize in conducting efficacy and proof of concept studies using mouse models for Alzheimer's and Parkinson's disease. In our search for innovation, we have integrated Amytracker 520 from Ebba Biotech into our research protocols, and the results have been exceptional. Amytracker 520 has significantly enhanced our ability to detect and analyse key pathological features in brain tissue. Specifically, we have successfully identified amyloid plaques, Tau tangles, Lewy body-like inclusions, and alpha-synuclein preformed fibrils (PFFs, which were administered stereotactically). The specificity of the stain, combined with... Read more →

Testimonial - Fabrizio Chiti

Prof. Fabrizio Chiti about Amytracker 630: "I like Amytracker probes because they can be used to detect amyloid-like species inside cells. We have used Amytracker 630 to exclude amyloid-like species of TDP-43 expressed in NSC34 cultured cells. We have also used cells treated with BSA and preformed Abeta fibrils as negative and positive controls respectively, all internalised with a specific kit. We detected fluorescence only in the latter case, as expected. Cells were fixed, permeabilized with Triton X-100 and Amytracker 630 was then added." Prof. Fabrizio Chiti is Full Professor of Biochemistry leading the Laboratory for the Study of Protein... Read more →

Testimonial - Adam Kreutzer

Adam Kreutzer about Amytracker 680: “I have been very happy with the Amytracker dyes I have used thus far. I have easily worked the Amytracker dyes into my free-floating, fixed brain tissue immunostaining workflow. The nice thing about the Amytracker dyes is that I don’t have to dehydrate the tissue in a series of ethanols and xylene, which is required for the widely used thioflavin and congo red dyes. The Amytracker dyes can just be applied to the tissue in TBS and then imaged. I often don’t even wash the tissues after treatment with the Amytracker dyes." Adam Kreutzer, PhD,... Read more →

Testimonial - Keiza Jack

Keiza Jack about Amytracker 540: “I have used Amytracker 540 in my PhD project as a tool to measure the structural differences of prion structures and prion-seeded amyloid fibrils. Amytracker 540 reports sensitively on subtle structural differences between protein structures, giving me a fast and reproduceable method to compare protein structures, which was essential to investigate my thesis" Kezia Jack from MRC Prion Unit, Institute of Prion Diseases, University College London, London, UK Testimonial given on November 10th, 2022 Read more →

Testimonial - Jaakko Sarparanta

Dr. Jaakko Sarparanta about Amytracker 680: ”We used Amytracker 680 to study the amyloid-like nature of pathological protein aggregates in muscle sections. The bright positive staining was easily interpreted and provided the much needed support for our Congo Red results.” Dr. Jaakko Sarparanta, Folkhälsan Research Center, Helsinki, Finland. Testimonial given on May 27th, 2021 Read more →

Testimonial - Megg Garcia

M. Garcia about Amytracker 520: "We are studying Alzheimer’s disease in mouse models and use a variety of anti-amyloid-beta antibodies and traditional dyes to look at amyloid-beta aggregation. Amytracker 520 gave a very clean staining with high signal to noise. It was easy to use as a part of routine immunohistochemistry and made for a great complement to Thioflavin S staining to detect dense-core plaques with much less background." M. Garcia (MSc), Doctoral student, Sweden Testimonial given on April 21st, 2021 Read more →

2026

  • Labra, S. R., Compher, J., Prabhavalkar, A., Almaraz, M., Cedeño Kwong, C., Baal, C., Talantova, M., Dolatabadi, N., Piña-Sanz, J., Wang, Y., Yoon, L., Ghatak, S., Gao, Z., Zhang, Y., Trudler, D., Massey, L., Lin, W., Balistreri, A., Bula, M., Schork, N., Mandala, T., Head, S., Kelly, J. & Lipton, S. A. (2026). Autophagy Activators Normalize Aberrant Tau Proteostasis and Rescue Synapses in Human Familial Alzheimer’s Disease iPSC-Derived Cortical Organoids. Advanced Science 13(17), e14783. https://doi.org/10.1002/ADVS.202514783
  • Featherby, S. J., Faulkner, E. C., Gordon, A., & Ettelaie, C. (2026). Procoagulant Extracellular Vesicles Increase Neuronal Tau expression, Metabolism and Processing Through Tissue Factor and Protease Activated Receptor 2. Cellular and Molecular Neurobiology 46(1), 21-. https://doi.org/10.1007/S10571-025-01658-7
  • da Silva, I. A. N., Paulus, A., Skoryk, V., Su, K. Y., Herranz-Trillo, F., & Klementieva, O. (2026). Polystyrene nanoplastic exposure promotes amyloid misfolding and metabolic impairment at sublethal doses. A subcellular infrared imaging study. Environmental Science: Nano 13(4), 1948–1961. https://doi.org/10.1039/D5EN01181G
  • Ariyath, A., Arigo, F. D., Wallach, I., Fernando, W. M. A. D. B., Martins, R. N., & Bharadwaj, P. (2026). Novel Small-Molecule Analogues of IU1 Ameliorate Amyloid-β Mediated Toxicity in Alzheimer’s Disease Cell and Worm Models. International Journal of Molecular Sciences 27(4), 1963. https://doi.org/10.3390/IJMS27041963/S1
  • de Schepper, S., Konstantellos, V., Conway, J. A., Sokolova, D., Zaccagnini, L., Cowley, M. v., Sierksma, A., Yudina, M., Edmonds, M., Gavriouchkina, D., Geary, B., Wallis, A., Celikag, M., Baykam, Z., Vara-Pérez, M., Crowley, G., Hager, F. T., Bijnen, M., Posner, D., Luk, K., Cerovic, V., Clatworthy, M., Videlock, E., Jaunmuktane, Z., Movahedi, K., Greater, M. Chain, B. Alessi, D., Hong, S. & Bartels, T. (2026). Intestinal macrophages modulate synucleinopathy along the gut–brain axis. Nature 651(8104), 174–184. https://doi.org/10.1038/s41586-025-09984-y
  • Ferreon, J. C., Choi, K. J., Quan, M. D., Tsoi, P. S., Ferreon, C. C., Coskun, U., Liao, S. C. J., & Ferreon, A. C. M. (2026). Modulation of Biomolecular Aggregate Morphology and Condensate Infectivity. Biomolecules 16(4), 492.https://doi.org/10.3390/BIOM16040492/S1
  • Fischer, C. M., Edu, I. A., Šneideris, T., Baronaite, I., Toprakcioglu, Z., Deck, L. T., Qian, D., Scrutton, R., Dreyer, L., Wen, J., Otzen, D. E., Wu, S., Perrett, S., & Knowles, T. P. J. (2026). Reversibility and β-sheet formation are decoupled in tau condensate aging. PNAS 16(4), 492. https://doi.org/10.1073/PNAS.2522993123

2025

  • Zattoni, M., Bernegger, S., Weinbender, S., Altendorfer, B., Mrowetz, H., Benedetti, A., Poupardin, R., Unger, M. S., & Aigner, L. (2025). The involvement of microglia and the CXCL16-CXCR6 axis in the recruitment of CD8+ T cells to an amyloidogenic mouse brain. Scientific Reports, 15(1), 38221-. https://doi.org/10.1038/s41598-025-22137-5
  • Altendorfer, B., Benedetti, A., Mrowetz, H., Bernegger, S., Bretl, A., Preishuber-Pflügl, J., Bessa de Sousa, D. M., Ladek, A. M., Koller, A., le Faouder, P., Bertrand-Michel, J., Trost, A., & Aigner, L. (2025). Omega-3 EPA Supplementation Shapes the Gut Microbiota Composition and Reduces Major Histocompatibility Complex Class II in Aged Wild-Type and APP/PS1 Alzheimer’s Mice: A Pilot Experimental Study. Nutrients, 17(7), 1108. https://doi.org/10.3390/nu17071108
  • Lee, J., Chin, N., Zou, J., Mazli, W. N. A. B., Jarnik, M., Saidi, L., Xu, Y., Jeong, E., Suh, J., Replogle, J., Ward, M. E., Bonifacino, J. S., Zheng, W., Hao, L., & Ye, Y. (2025). CHIP protects lysosomes from CLN4 mutant-induced membrane damage. Nature Cell Biology, 27(9), 1465–1481. https://doi.org/10.1038/S41556-025-01738-2
  • Urbanek, A., Garland, E. F., Prescott, E. E., King, M. C., Olerinyova, A., Wareing, H. E., Georgieva, N., Bradshaw, E. L., Tzokov, S. B., Knight, A., Tartakovskii, A. I., Malm, T., Highley, J. R., & De, S. (2025). Molecular Determinants of Protein Pathogenicity at the Single-Aggregate Level. Advanced Science, 15(8). https://doi.org/10.1002/ADVS.202410229
  • do Amaral, M. J., Passos, A. R., Mohapatra, S., Freire, M. H., Wegmann, S., & Cordeiro, Y. (2025). X-Ray Photon Correlation Spectroscopy, Microscopy, and Fluorescence Recovery After Photobleaching to Study Phase Separation and Liquid-to-Solid Transition of Prion Protein Condensates. Bio-Protocol, 15(8). https://doi.org/10.21769/BIOPROTOC.5277
  • Zhan, X., Li, W., Hatterer, E., Courade, J. P., Piché, K., Klementieva, O., & Li, J. Y. (2025). Strain-Distinct α-Synuclein and Tau Cross-Seeding Uncovered by Correlative Approach with Optical Photothermal Infrared Sub-Micron Imaging. Journal of the American Chemical Society, 147(31), 27323–27340. https://doi.org/10.1021/JACS.5C02811
  • Horvath, I., Aning, O. A., Kk, S., Rehnberg, N., Chawla, S., Molin, M., Westerlund, F., & Wittung-Stafshede, P. (2025). Biological Amyloids Chemically Damage DNA. ACS Chemical Neuroscience, 16(3), 355–364. https://doi.org/10.1021/ACSCHEMNEURO.4C00461
  • Puthia, M., Marzinek, J. K., Vesela, K., Larsson, A., Schmidtchen, A., Bond, P. J., &amp Petrlova, J. (2025). Apolipoprotein E3 and E4 isoforms exhibit differing effects in countering endotoxins. Journal of Biological Chemistry, 301(3), 108236. https://doi.org/10.1016/j.jbc.2025.108236
  • Nozohouri, E., Noorani, B., Patel, D., Ahn, Y., Zoubi, S., & Bickel, U. (2025). Assessing blood-brain barrier (BBB) integrity in an Alzheimer’s disease mouse model: is the BBB globally or locally disrupted? Fluids and Barriers of the CNS, 22(1), 79. https://doi.org/10.1186/S12987-025-00685-2
  • Qin, J., Yang, Q., Ullate-Agote, A., Sampaio-Pinto, V., Florit, L., Dokter, I., Mathioudaki, C., Middelberg, L., Montero-Calle, P., Aguirre-Ruiz, P., de las Heras Rojo, J., Lei, Z., Qiu, Z., Wei, J., van der Harst, P., Prosper, F., Mazo, M. M., Iglesias-García, O., Minnema, M. C., … van Mil, A. (2025). Uncovering cell type-specific phenotypes using a novel human in vitro model of transthyretin amyloid cardiomyopathy. Stem Cell Research & Therapy 2025 16:1, 16(1), 1–17. https://doi.org/10.1186/S13287-025-04464-6
  • Kunnath, S. M., Arad, E., Zalk, R., Kass, I., Shahar, A., Batushansky, A., Rapaport, H., & Jelinek, R. (2025). Allosteric amyloid catalysis by coiled coil fibrils. Nature Communications, 16(1), 5071-. https://doi.org/10.1038/s41467-025-60379-z
  • Yan, X., Kuster, D., Mohanty, P., Nijssen, J., Pombo-García, K., Garcia Morato, J., Rizuan, A., Franzmann, T. M., Sergeeva, A., Ly, A. M., Liu, F., Passos, P. M., George, L., Wang, S. H., Shenoy, J., Danielson, H. L., Ozguney, B., Honigmann, A., Ayala, Y. M., … Hyman, A. A. (2025). Intra-condensate demixing of TDP-43 inside stress granules generates pathological aggregates. Cell, 188(15), 4123-4140.e18. https://doi.org/10.1016/J.CELL.2025.04.039
  • Feng, J., Osmekhina, E., Timonen, J. V. I., & Linder, M. B. (2025). Effects of Sup35 overexpression on the formation, morphology, and physiological functions of intracellular Sup35 assemblies. Applied and Environmental Microbiology, 91(3). https://doi.org/10.1128/AEM.01703-24
  • Olari, L. R., Liu, S., Arnold, F., Kühlwein, J., Gil Miró, M., Updahaya, A. R., Stürzel, C., Thal, D. R., Walther, P., Sparrer, K. M. J., Danzer, K. M., Münch, J., & Kirchhoff, F. (2025). α-Synuclein fibrils enhance HIV-1 infection of human T cells, macrophages and microglia. Nature Communications, 16(1), 1–18. https://doi.org/10.1038/s41467-025-56099-z
  • Huang, M., & McEwan, W. A. (2025). Sensitive detection and propagation of brain-derived tau assemblies in HEK293-based wild-type tau seeding assays. Journal of Biological Chemistry, 301(3), 108245. https://doi.org/10.1016/j.jbc.2025.108245

2024

  • Sanislav, O., Tetaj, R., Metali, Ratcliffe, J., Phillips, W., Klein, A. R., Sethi, A., Zhou, J., Mezzenga, R., Saxer, S. S., Charnley, M., Annesley, S. J., & Reynolds, N. P. (2024). Cell invasive amyloid assemblies from SARS-CoV-2 peptides can form multiple polymorphs with varying neurotoxicity. Nanoscale, 16(42), 19814–19827. https://doi.org/10.1039/D4NR03030C
  • Eroglu, M., Zocher, A., McAuley, J., Webster, R., Xiao, M. Z. X., Yu, B., Mok, C., & Derry, W. B. (2024). Noncanonical inheritance of phenotypic information by protein amyloids. Nature Cell Biology, 26(11), 1712–1724. https://doi.org/10.1038/s41556-024-01494-9
  • Koundal, S., Chen, X., Gursky, Z., Lee, H., Xu, K., Liang, F., Xie, Z., Xu, F., Lin, H. M., van Nostrand, W. E., Gu, X., Elkin, R., Tannenbaum, A., & Benveniste, H. (2024). Divergent brain solute clearance in rat models of cerebral amyloid angiopathy and Alzheimer’s disease. IScience, 27(12), 111463. https://doi.org/10.1016/j.isci.2024.111463
  • Farzadfard, A., Mason, T. O., Kunka, A., Mohammad-Beigi, H., Bjerregaard-Andersen, K., Folke, J., Aznar, S., Kallunki, P., & Buell, A. K. (2025). The Amplification of Alpha-Synuclein Amyloid Fibrils is Suppressed under Fully Quiescent Conditions. Angewandte Chemie International Edition, 64(7), e202419173. https://doi.org/10.1002/ANIE.202419173
  • Hurtle, B., Donnelly, C. J., Zhang, X., & Thathiah, A. (2024). Live-cell visualization of tau aggregation in human neurons. Communications Biology, 7(1), 1–11. https://doi.org/10.1038/s42003-024-06840-z
  • Pinzi, L., Conze, C., Bisi, N., Torre, G. D., Soliman, A., Monteiro-Abreu, N., Trushina, N. I., Krusenbaum, A., Dolouei, M. K., Hellwig, A., Christodoulou, M. S., Passarella, D., Bakota, L., Rastelli, G., & Brandt, R. (2024). Quantitative live cell imaging of a tauopathy model enables the identification of a polypharmacological drug candidate that restores physiological microtubule interaction. Nature Communications, 15(1), 1679. https://doi.org/10.1038/s41467-024-45851-6
  • Šulskis, D., Žiaunys, M., Sakalauskas, A., Sniečkute, R., & Smirnovas, V. (2024). Formation of amyloid fibrils by the regulatory 14-3-3ζ protein. Open Biology, 14(1). https://doi.org/10.1098/rsob.230285
  • Dranseike, D., Ota, Y., Edwardson, T. G. W., Guzzi, E. A., Hori, M., Nakic, Z. R., Deshmukh, D. v., Levasseur, M. D., Mattli, K., Tringides, C. M., Zhou, J., Hilvert, D., Peters, C., & Tibbitt, M. W. (2024). Designed modular protein hydrogels for biofabrication. Acta Biomaterialia, 177, 107–117. https://doi.org/10.1016/J.ACTBIO.2024.02.019
  • Balana, A. T., Mahul-Mellier, A. L., Nguyen, B. A., Horvath, M., Javed, A., Hard, E. R., Jasiqi, Y., Singh, P., Afrin, S., Pedretti, R., Singh, V., Lee, V. M. Y., Luk, K. C., Saelices, L., Lashuel, H. A., & Pratt, M. R. (2024). O-GlcNAc forces an α-synuclein amyloid strain with notably diminished seeding and pathology. Nature Chemical Biology, 20(5), 646–655. https://doi.org/10.1038/s41589-024-01551-2
  • Kreutzer, A. G., Parrocha, C. M. T., Haerianardakani, S., Guaglianone, G., Nguyen, J. T., Diab, M. N., Yong, W., Perez-Rosendahl, M., Head, E., & Nowick, J. S. (2024). Antibodies Raised Against an Aβ Oligomer Mimic Recognize Pathological Features in Alzheimer’s Disease and Associated Amyloid-Disease Brain Tissue. ACS Central Science, 10(1), 104–121. https://doi.org/10.1021/acscentsci.3c00592
  • Raymundo, J. R., Zhang, H., Smaldone, G., Zhu, W., Daly, K. E., Glennon, B. J., Pecoraro, G., Salvatore, M., Devine, W. A., Lo, C. W., Vitagliano, L., & Marneros, A. G. (2024). KCTD1/KCTD15 complexes control ectodermal and neural crest cell functions, and their impairment causes aplasia cutis. The Journal of Clinical Investigation, 134(4). https://doi.org/10.1172/JCI174138
  • Morelli, C., Faltova, L., Capasso Palmiero, U., Makasewicz, K., Papp, M., Jacquat, R. P. B., Pinotsi, D., & Arosio, P. (2024). RNA modulates hnRNPA1A amyloid formation mediated by biomolecular condensates. Nature Chemistry, 16(7), 1052–1061. https://doi.org/10.1038/s41557-024-01467-3
  • Kitamura, A., Fujimoto, A., Kawashima, R., Lyu, Y., Sasaki, K., Hamada, Y., Moriya, K., Kurata, A., Takahashi, K., Brielmann, R., Bott, L. C., Morimoto, R. I., & Kinjo, M. (2024). Hetero-oligomerization of TDP-43 carboxy-terminal fragments with cellular proteins contributes to proteotoxicity. Communications Biology, 7(1). https://doi.org/10.1038/s42003-024-06410-3
  • de Oliveira, D. H., Gowda, V., Sparrman, T., Gustafsson, L., Sanches Pires, R., Riekel, C., Barth, A., Lendel, C., & Hedhammar, M. (2024). Structural conversion of the spidroin C-terminal domain during assembly of spider silk fibers. Nature Communications, 15(1). https://doi.org/10.1038/s41467-024-49111-5
  • Sun, H., Yang, B., Li, Q., Zhu, X., Song, E., Liu, C., Song, Y., & Jiang, G. (2024). Polystyrene nanoparticles trigger aberrant condensation of TDP-43 and amyotrophic lateral sclerosis-like symptoms. Nature Nanotechnology. https://doi.org/10.1038/s41565-024-01683-5
  • Li, B., Suresh, P., Brelstaff, J., Kedia, S., Bryant, C. E., & Klenerman, D. (2024). The delayed kinetics of Myddosome formation explains why amyloid-beta aggregates trigger Toll-like receptor 4 less efficiently than lipopolysaccharide. eLife, 13, RP92350. https://doi.org/10.7554/eLife.92350
  • Bacioglu, M., Schweighauser, M., Gray, D., Lövestam, S., Katsinelos, T., Quaegebeur, A., van Swieten, J., Jaunmuktane, Z., Davies, S. W., Scheres, S. H. W., Goedert, M., Ghetti, B., & Spillantini, M. G. (2024). Cleaved TMEM106B forms amyloid aggregates in central and peripheral nervous systems. Acta Neuropathologica Communications, 12(1). https://doi.org/10.1186/s40478-024-01813-z
  • Eltom, K., Mothes, T., Libard, S., Ingelsson, M., & Erlandsson, A. (2024). Astrocytic accumulation of tau fibrils isolated from Alzheimer’s disease brains induces inflammation, cell-to-cell propagation and neuronal impairment. Acta Neuropathologica Communications, 12(1). https://doi.org/10.1186/s40478-024-01745-8

2023

  • Arad, E., Pedersen, K. B., Malka, O., Mambram Kunnath, S., Golan, N., Aibinder, P., Schiøtt, B., Rapaport, H., Landau, M., & Jelinek, R. (2023). Staphylococcus aureus functional amyloids catalyze degradation of β-lactam antibiotics. Nature Communications, 14(1). https://doi.org/10.1038/s41467-023-43624-1
  • Juliani do Amaral, M., Mohapatra, S., Ribeiro Passos, A., Sousa Lopes da Silva, T., Sampaio Carvalho, R., da Silva Almeida, M., Sá Pinheiro, A., Wegmann, S., & Cordeiro, Y. (2023). Copper drives prion protein phase separation and modulates aggregation. Science Advances, 9, eadi7347. https://doi.org/10.1126/sciadv.adi7347
  • Chandhok, S., Pereira, L., Momchilova, E. A., Marijan, D., Zapf, R., Lacroix, E., Kaur, A., Keymanesh, S., Krieger, C., & Audas, T. E. (2023). Stress-mediated aggregation of disease-associated proteins in amyloid bodies. Scientific Reports, 13(1). https://doi.org/10.1038/s41598-023-41712-2
  • Chia, S., Faidon Brotzakis, Z., Horne, R. I., Possenti, A., Mannini, B., Cataldi, R., Nowinska, M., Staats, R., Linse, S., Knowles, T. P. J., Habchi, J., & Vendruscolo, M. (2023). Structure-Based Discovery of Small-Molecule Inhibitors of the Autocatalytic Proliferation of α-Synuclein Aggregates. Mol. Pharmaceutics, 20, 183–193. https://doi.org/10.1021/acs.molpharmaceut.2c00548
  • Frenkel, A., Zecharia, E., Gómez-Pérez, D., Sendersky, E., Yegorov, Y., Jacob, A., Benichou, J. I. C., Stierhof, Y. D., Parnasa, R., Golden, S. S., Kemen, E., & Schwarz, R. (2023). Cell specialization in cyanobacterial biofilm development revealed by expression of a cell-surface and extracellular matrix protein. Npj Biofilms and Microbiomes 2023 9:1, 9(1), 1–10. https://doi.org/10.1038/s41522-023-00376-6
  • Gvazava, N., Konings, S. C., Cepeda-Prado, E., Skoryk, V., Umeano, C. H., Dong, J., Silva, I. A. N., Ottosson, D. R., Leigh, N. D., Wagner, D. E., & Klementieva, O. (2023). Label-Free High-Resolution Photothermal Optical Infrared Spectroscopy for Spatiotemporal Chemical Analysis in Fresh, Hydrated Living Tissues and Embryos. Journal of the American Chemical Society. https://doi.org/10.1021/jacs.3c08854
  • Petrlova, J., Hartman, E., Petruk, G., Lim, J. C. H., Adav, S. S., Kjellström, S., Puthia, M., & Schmidtchen, A. (2023). Selective protein aggregation confines and inhibits endotoxins in wounds: Linking host defense to amyloid formation. iScience, 26(10). https://doi.org/10.1016/j.isci.2023.107951
  • Kommaddi, R. P., Verma, A., Muniz-Terrera, G., Tiwari, V., Chithanathan, K., Diwakar, L., Gowaikar, R., Karunakaran, S., Malo, P. K., Graff-Radford, N. R., Day, G. S., Laske, C., Vöglein, J., Nübling, G., Ikeuchi, T., Kasuga, K., & Ravindranath, V. (2023). Sex difference in evolution of cognitive decline: studies on mouse model and the Dominantly Inherited Alzheimer Network cohort. Translational Psychiatry, 13(1), 1–12. https://doi.org/10.1038/s41398-023-02411-8
  • Ornithopoulou, E., Åstrand, C., Gustafsson, L., Crouzier, T., & Hedhammar, M. (2023). Self-Assembly of RGD-Functionalized Recombinant Spider Silk Protein into Microspheres in Physiological Buffer and in the Presence of Hyaluronic Acid. ACS Applied Bio Materials, 6(9), 3696–3705. https://doi.org/10.1021/acsabm.3c00373
  • Piroska, L., Fenyi, A., Thomas, S., Plamont, M.-A., Redeker, V., Melki, R., & Gueroui, Z. (2023). α-Synuclein liquid condensates fuel fibrillar α-synuclein growth. Science Advances, 9(33), eadg5663. https://doi.org/10.1126/sciadv.adg5663
  • Prater, C., Bai, Y., Konings, S. C., Martinsson, I., Swaminathan, V. S., Nordenfelt, P., Gouras, G., Borondics, F., & Klementieva, O. (2023). Fluorescently Guided Optical Photothermal Infrared Microspectroscopy for Protein-Specific Bioimaging at Subcellular Level. Journal of Medicinal Chemistry, 66(4), 2542–2549. https://doi.org/10.1021/acs.jmedchem.2c01359

2022

  • Cascella, R., Banchelli, M., Abolghasem Ghadami, S., Ami, D., Gagliani, M. C., Bigi, A., Staderini, T., Tampellini, D., Cortese, K., Cecchi, C., Natalello, A., Adibi, H., Matteini, P., & Chiti, F. (2022). An in situ and in vitro investigation of cytoplasmic TDP-43 inclusions reveals the absence of a clear amyloid signature. Annals of Medicine, 55(1), 72–88. https://doi.org/10.1080/07853890.2022.2148734
  • Choi, M. L., Chappard, A., Singh, B. P., Maclachlan, C., Abramov, A. Y., Horrocks, M. H., & Gandhi, S. (2022). Pathological structural conversion of α-synuclein at the mitochondria induces neuronal toxicity. Nature Neuroscience. https://doi.org/10.1038/s41593-022-01140-3
  • de Luca, C. M. G., Consonni, A., Cazzaniga, F. A., Bistaffa, E., Bufano, G., Quitarrini, G., Celauro, L., Legname, G., Eleopra, R., Baggi, F., Giaccone, G., & Moda, F. (2022). The alpha-synuclein RT-QuIC products generated by the olfactory mucosa of patients with parkinson’s disease and multiple system atrophy induce inflammatory responses in SH-SY5Y cells. Cells, 11(1). https://doi.org/10.3390/cells11010087
  • Wood, J. I., Wong, E., Cummings, D. M., Hardy, J., Correspondence, F. A. E., Joghee, R., Balbaa, A., Vitanova, K. S., Stringer, K. M., Vanshoiack, A., Phelan, S.-L. J., Launchbury, F., Desai, S., Tripathi, T., Rg Hanrieder, J., & Edwards, F. A. (2022). Plaque contact and unimpaired Trem2 is required for the microglial response to amyloid pathology. Cell Reports. https://doi.org/10.1016/j.celrep.2022.111686
  • Petrlova, J., Samsudin, F., Bond, P. J., & Schmidtchen, A. (2022). SARS-CoV-2 spike protein aggregation is triggered by bacterial lipopolysaccharide. FEBS Letters. https://doi.org/10.1002/1873-3468.14490
  • Morten, M. J., Sirvio, L., Rupawala, H., Hayes, E. M., Franco, A., Radulescu, C., Ying, L., Barnes, S. J., Muga, A., & Ye, Y. (2022). Quantitative super-resolution imaging of pathological aggregates reveals distinct toxicity profiles in different synucleinopathies. PNAS. https://doi.org/10.1073/pnas.2205591119
  • Hochmair, J., Exner, C., Franck, M., Dominguez‐Baquero, A., Diez, L., Brognaro, H., Kraushar, M. L., Mielke, T., Radbruch, H., Kaniyappan, S., Falke, S., Mandelkow, E., Betzel, C., & Wegmann, S. (2022). Molecular crowding and RNA synergize to promote phase separation, microtubule interaction, and seeding of Tau condensates. The EMBO Journal, 41(11). https://doi.org/10.15252/EMBJ.2021108882
  • Kumar, S. T., Mahul-Mellier, A. L., Hegde, R. N., Rivière, G., Moons, R., de Opakua, A. I., Magalhães, P., Rostami, I., Donzelli, S., Sobott, F., Zweckstetter, M., & Lashuel, H. A. (2022). A NAC domain mutation (E83Q) unlocks the pathogenicity of human alpha-synuclein and recapitulates its pathological diversity. Science Advances, 8(17), 44. https://doi.org/10.1126/SCIADV.ABN0044
  • Lackie, R. E., de Miranda, A. S., Lim, M. P., Novikov, V., Madrer, N., Karunatilleke, N. C., Rutledge, B. S., Tullo, S., Brickenden, A., Maitland, M. E. R., Greenberg, D., Gallino, D., Luo, W., Attaran, A., Shlaifer, I., del Cid Pellitero, E., Schild-Poulter, C., Durcan, T. M., Fon, E. A., … Prado, M. A. M. (2022). Stress-inducible phosphoprotein 1 (HOP/STI1/STIP1) regulates the accumulation and toxicity of α-synuclein in vivo. Acta Neuropathologica. https://doi.org/10.1007/s00401-022-02491-8

2021

  • Graziotto, M. E., Adair, L. D., Kaur, A., Vérité, P., Ball, S. R., Sunde, M., Jacquemin, D., & New, E. J. (2021). Versatile naphthalimide tetrazines for fluorogenic bioorthogonal labelling. RSC Chemical Biology, 2(5), 1491–1498. https://doi.org/10.1039/D1CB00128K
  • Michno, W., Stringer, K. M., Enzlein, T., Passarelli, M. K., Escrig, S., Vitanova, K., Wood, J., Blennow, K., Zetterberg, H., Meibom, A., Hopf, C., Edwards, F. A., & Hanrieder, J. (2021). Following spatial Aβ aggregation dynamics in evolving Alzheimer’s disease pathology by imaging stable isotope labeling kinetics. Science Advances, 7(25), 4855–4871. https://doi.org/10.1126/SCIADV.ABG4855/
  • Aubi, O., Prestegård, K. S., Jung-KC, K., Shi, T. J. S., Ying, M., Grindheim, A. K., Scherer, T., Ulvik, A., McCann, A., Spriet, E., Thöny, B., & Martinez, A. (2021). The Pah-R261Q mouse reveals oxidative stress associated with amyloid-like hepatic aggregation of mutant phenylalanine hydroxylase. Nature Communications 2021 12:1, 12(1), 1–16. https://doi.org/10.1038/s41467-021-22107-1
  • Frey, B., AlOkda, A., Jackson, M. P., Riguet, N., Duce, J. A., & Lashuel, H. A. (2021). Monitoring alpha-synuclein oligomerization and aggregation using bimolecular fluorescence complementation assays: What you see is not always what you get. Journal of Neurochemistry, 157(4), 872–888. https://doi.org/10.1111/jnc.15147
  • Frottin, F., Pérez-Berlanga, M., Hartl, F. U., & Hipp, M. S. (2021). Multiple pathways of toxicity induced by C9orf72 dipeptide repeat aggregates and G4C2 RNA in a cellular model. ELife, 10. https://doi.org/10.7554/eLife.62718
  • Rimal, S., Li, Y., Vartak, R., Geng, J., Tantray, I., Li, S., Huh, S., Vogel, H., Glabe, C., Grinberg, L. T., Spina, S., Seeley, W. W., Guo, S., & Lu, B. (2021). Inefficient quality control of ribosome stalling during APP synthesis generates CAT-tailed species that precipitate hallmarks of Alzheimer’s disease. Acta Neuropathologica Communications, 9(1), 1–24. https://doi.org/10.1186/s40478-021-01268-6
  • Hofbauer, D., Mougiakakos, D., Mackensen, A., Ricagno, S., & Bruns, H. (2021). B2-microglobulin triggers NLRP3 inflammasome activation in tumor-associated macrophages to promote multiple myeloma progression. Immunity. https://doi.org/10.1016/j.immuni.2021.07.002
  • Johari, M., Sarparanta, J., Vihola, A., Jonson, P. H., Savarese, M., Jokela, M., Torella, A., Piluso, G., Said, E., Vella, N., Cauchi, M., Magot, A., Magri, F., Mauri, E., Kornblum, C., Reimann, J., Stojkovic, T., Romero, N. B., Luque, H., Huovinen, S., Lahermo, P., Donner, K., Comi, G. P., Nigro, V., Hackman, P., & Udd, B. (2021). Missense mutations in small muscle protein X-linked (SMPX) cause distal myopathy with protein inclusions. Acta Neuropathologica, 0123456789. https://doi.org/10.1007/s00401-021-02319-x

2020

  • Mahul-Mellier, A. L., Burtscher, J., Maharjan, N., Weerens, L., Croisier, M., Kuttler, F., Leleu, M., Knott, G. W., & Lashuel, H. A. (2020). The process of Lewy body formation, rather than simply α-synuclein fibrillization, is one of the major drivers of neurodegeneration. Proceedings of the National Academy of Sciences of the United States of America, 117(9), 4971–4982. https://doi.org/10.1073/pnas.1913904117
  • Ghosh, A., Mizuno, K., Tiwari, S. S., Proitsi, P., Gomez Perez-Nievas, B., Glennon, E., Martinez-Nunez, R. T., & Giese, K. P. (2020). Alzheimer’s disease-related dysregulation of mRNA translation causes key pathological features with ageing. Translational Psychiatry, 10(1), 1–18. https://doi.org/10.1038/s41398-020-00882-7

2019

  • Page, M. J., Thomson, G. J. A., Nunes, J. M., Engelbrecht, A. M., Nell, T. A., de Villiers, W. J. S., de Beer, M. C., Engelbrecht, L., Kell, D. B., & Pretorius, E. (2019). Serum amyloid A binds to fibrin(ogen), promoting fibrin amyloid formation. Scientific Reports, 9(1), 1–14. https://doi.org/10.1038/s41598-019-39056-x
  • Adams, B., Nunes, J. M., Page, M. J., Roberts, T., Carr, J., Nell, T. A., Kell, D. B., & Pretorius, E. (2019). Parkinson’s disease: A systemic inflammatory disease accompanied by bacterial inflammagens. Frontiers in Aging Neuroscience, 10(JUL), 1–17. https://doi.org/10.3389/fnagi.2019.00210
  • Frottin, F., Schueder, F., Tiwary, S., Gupta, R., Körner, R., Schlichthaerle, T., Cox, J., Jungmann, R., Hartl, F. U., & Hipp, M. S. (2019). The nucleolus functions as a phase-separated protein quality control compartment. Science, 365(6451), 342–347. https://doi.org/10.1126/science.aaw9157

2018

  • de Waal, G. M., Engelbrecht, L., Davis, T., de Villiers, W. J. S., Kell, D. B., & Pretorius, E. (2018). Correlative Light-Electron Microscopy detects lipopolysaccharide and its association with fibrin fibres in Parkinson’s Disease, Alzheimer’s Disease and Type 2 Diabetes Mellitus. Scientific Reports, 8(1), 1–12. https://doi.org/10.1038/s41598-018-35009-y
  • Pretorius, E., Page, M. J., Hendricks, L., Nkosi, N. B., Benson, S. R., & Kell, D. B. (2018). Both lipopolysaccharide and lipoteichoic acids potently induce anomalous fibrin amyloid formation: Assessment with novel Amytracker TM stains. Journal of the Royal Society Interface, 15(139). https://doi.org/10.1098/rsif.2017.0941

2017

  • Sehlin, D., Fang, X. T., Meier, S. R., Jansson, M., & Syvänen, S. (2017). Pharmacokinetics, biodistribution and brain retention of a bispecific antibody-based PET radioligand for imaging of amyloid-β. Scientific Reports, 7(1), 1–9. https://doi.org/10.1038/s41598-017-17358-2
  • Pretorius, E., Page, M. J., Engelbrecht, L., Ellis, G. C., & Kell, D. B. (2017). Substantial fibrin amyloidogenesis in type 2 diabetes assessed using amyloid-selective fluorescent stains. Cardiovascular Diabetology, 16(1), 1–14. https://doi.org/10.1186/s12933-017-0624-5

Amytracker fluorescence spectra

We named our Amytracker molecules after their peak emission wavelength when they are bound to their target. That means, when Amytracker is bound to a target, it will emit fluorescence at peak emission indicated by the number associated with its name.

To view the excitation and emission spectra, please select your Amytracker below :

Excitation (blue lines) and emission (red lines) spectra of unbound Amytracker (dotted lines) and Amytracker bound to a target (solid lines).
Labeling of protein aggregates in tissue sections or cells

Labeling of protein aggregates in tissue sections or cells

Amytracker can be used to label protein aggregates in tissue sections or cells prepared by the most common techniques. It can be used in freshly sliced tissue without fixation but also in fixed cells or sections obtained from flash-frozen or paraffin embedded tissues. Generally, fixation in 4% PFA works well for extracellular deposits, and fixation in ice-cold ethanol or acetone is recommended for best preservation of intracellular aggregates. Amytracker can be easily combined with your co-staining of choice. As Amytracker are only fluorescent when bound to their target, washing steps might be omitted and it is possible to add Amytracker... Read more →
Amytracker for systemic injection

Amytracker for systemic injection

Amytracker can be used for intravenous- or intraperitoneal injection in small animals to label protein aggregates in vivo. It will readily cross the blood brain barrier and can be imaged by intra-vital microscopy or after removing the tissue and preparation of microscope slides. For systemic injection, we recommend to use our Amytracker - Solid formulation that comes in sterile injection bottles. Solutions and Reagents: Amytracker - Solid 1mg Physiological saline Injection syringes and needles Assay Procedure: Add 250 µl physiological saline to the Amytracker - 1mg Solid by injecting it directly through the rubber stopper. Dissolve all powder residues by... Read more →
Fibrillation assay

Fibrillation assay

This protocol describes how Amytracker can be utilized for fibrillation assays and detection of amyloids in liquid samples. As all Amytracker variants are highly fluorescent only when they are bound to their target, they are ideally suited for spectrophotometric analysis. We recommend to perform a titration to use Amytracker in the lowest concentration possible for your specific application. The experimental conditions used to induce protein misfolding and aggregation can vary considerably depending on the amyloidogenic protein or peptide. It is important to note that Amytracker fluorescence can vary depending on pH and ionic strength of the buffer. In this protocol,... Read more →
Live-cell imaging

Live-cell imaging

All Amytracker variants cross the cell membrane of living cells without permeabilization. Due to their low background fluorescence and minimal interference with biological autofluorescence, we recommend Amytracker 630 or Amytracker 680 for live-cell imaging. As Amytracker do not bleach easily, they are excellently suited for repeated illumination during time-lapse imaging. If possible, use serum-free medium during incubation. Solutions and Reagents: Amytracker - Aqueous or Amytracker - DMSO Imaging medium: Serum- and Phenol Red free cell culture medium Assay Procedure: Dilute Amytracker in Imaging medium 1:1000. Incubate your cells in Imaging medium for 30 min under normal culture conditions. Image cells... Read more →
Studying Spider Silk using Amytracker

Studying Spider Silk using Amytracker

Spider silk is an exceptional biomaterial known for centuries and used in medicine as suture threads and wound dressing thanks to its tensile strength, thinness and biocompatibility. Many of the properties of spider silk are a direct consequence of the structure and organization of spidroins, the proteins that make up the fiber. Spidroins contain high fractions of hydrophobic amino acids and repetitive sequences, which shift from an alpha-helical structure in solution to a beta-sheet assembly forming fibrils. This assembly transition is guided by the terminal regions of the spidroid proteins. However, natural production of spider silk is unsustainable as spiders... Read more →
Amytracker in action for Neuroprotection

Amytracker in action for Neuroprotection

With an aging population, neurological conditions such as Alzheimer’s disease (AD), Parkinson’s disease (PD), amyotrophic lateral sclerosis (ALS), and stroke affect millions worldwide, with projections suggesting a steep rise of cases by 2050. While some of these conditions are treatable, many remain without a cure. Neuroprotection - preserving the structure and function of neurons amidst ongoing damage - relies on a deep understanding of pathological processes, like protein aggregation and inflammation. Over the years scientists have attempted to reduce protein aggregation, control oxidative stress, and manage neuroinflammation. However, these approaches often fall short due to the brain’s complex architecture, which... Read more →
Studying the inflammation-aggregation connection using Amytracker

Studying the inflammation-aggregation connection using Amytracker

By 2050, the number of people aged >65 is expected to double. This will lead to a significant rise in the prevalence of age-related diseases. Many of these conditions are linked to two major processes: protein aggregation and chronic inflammation. The precise relationship between these two components and how they contribute to the pathology of age-related diseases remains unclear. It is uncertain whether protein aggregation triggers inflammation, or if inflammation drives the aggregation process. To date, anti-amyloid therapies, which were designed to reduce protein aggregation, have not delivered the hoped-for results in clinical trials. Instead, targeting the pro-inflammatory signalling pathways... Read more →

Multi-Laser / Multi-Detector Imaging with Amytracker

Amytracker are optotracers with structure-dependent photo-physical properties. All Amytracker variants are designed to bind to the Congo red binding pocket on the amyloid fibril and require a theoretical minimum of eight in-register parallel-β-strands for binding. Therefore, Amytracker reliably labels amyloids derived from a variety of amyloidogenic proteins or peptides from different species. Due to their structure-dependent photo physical properties, the Amytracker variants are only fluorescent when binding to a target and different targets can produce a difference in the molecules fluorescence spectrum. To investigate different targets, we recommend to perform imaging by exciting the sample with different wavelengths collecting fluorescence... Read more →

Optotracing using Amytracker

Amytracker are optotracers with structure-dependent photo-physical properties. All Amytracker variants are designed to bind to the Congo red binding pocket on the amyloid fibril and require a theoretical minimum of eight in-register parallel-β-strands for binding. Therefore, Amytracker reliably labels amyloids derived from a variety of amyloidogenic proteins or peptides from different species. Due to their structure-dependent photo-physical properties, the Amytracker variants are only fluorescent when binding to a target and different targets can produce a difference in the molecules fluorescence spectrum. To investigate different targets, we recommend collecting excitation and emission spectra with excitation and emission parameters summarised in the... Read more →
Amytracker and Long Covid

Amytracker and Long Covid

Around 30% of the people infected with the SARS-CoV-2 virus report persistent symptoms for a long time after the acute infection ends. While the development of this long-term manifestation after COVID, referred to as Long COVID, has been framed as mysterious, it is actually a well described outcome of many viral or bacterial infections. In the case of Long COVID, the chronic symptoms include shortness of breath, fatigue, chest pain, headaches, “brain fog”, and a procoagulant state. However common, it is not clear how the virus mediates these prolonged effects. Several hypotheses have been proposed to try and explain the... Read more →
Amytracker and the age-pigment Lipofuscin

Amytracker and the age-pigment Lipofuscin

The macromolecules and organelles within cells are not permanent and need to get replaced over time. To do this, cells need to both produce new components and to degrade the old ones. The degradation of the bigger cellular structures depends on a process called autophagy. During autophagy, the cell envelopes the to-be-destroyed organelle and uses lysosomes to digest it down to its basic components (amino acids, sugars, lipids, etc.). Unfortunately, lysosomes cannot completely degrade all the substances the organelles are made of, and this defect results over time in the formation of lipofuscin. In cells that are actively dividing, lipofuscin... Read more →
Amytracker for the study of tau aggregates

Amytracker for the study of tau aggregates

Tau is an intracellular protein which associates with microtubules and stabilizes them. Physiologically, Tau is phosphorylated to facilitate release from the microtubules and thereby favor microtubule shortening. In a pathological state, Tau is hyperphosphorylated which increases its tendency to aggregate in the cytoplasm. This means that conditions which promote abnormal phosphorylation of Tau promote its aggregation. Aggregates of hyperphosphorylated Tau form insoluble filaments and tangled clumps. These intracellular deposits are called Neurofibrillary tangles (NFTs). In the literature, predecessors of Amytracker have been used to label NFTs in tissue sections. It was found that the signal co-localises with the signal from... Read more →
Amytracker for studying α-synuclein aggregates

Amytracker for studying α-synuclein aggregates

Aggregates of α-synuclein are the major component of Lewy bodies which are the pathological hallmark of a series of neurodegenerative disorders, called Lewy body diseases or Synucleinopathies. In physiological conditions, α-synuclein regulates synaptic vesicle-release and possibly cytoskeletal assembly. However, this small pre-synaptic protein is characterized by an intrinsically disordered structure that makes it prone to aggregation. When aggregated, α-synuclein can interact with membranes and, for instance, make neurotransmitter vesicles “leaky”. This is especially important in dopaminergic neurons, as the interaction between dopamine and α-synuclein seems to further facilitate its oligomerization. When aggregated, α-synuclein cannot be disposed of by the cellular... Read more →
When proteins get out of shape

When proteins get out of shape

Human cells typically assemble a myriad of different proteins which constitute the work-force of the cellular environment and each of them is dedicated to a very specific function. The ability of a protein to perform its task is closely related to its structure: pockets, arms, and fingers are needed to store, move, and grasp molecules and other proteins resembling the workings of tiny biological machines. All proteins are translated from messenger RNA into a sequence of amino acids. In order to perform their specific task, they have to fold and assemble into a specific three-dimensional structure. The instructions for proper... Read more →
Are amyloid structures in abnormal blood clots a risk factor for amyloidosis?

Are amyloid structures in abnormal blood clots a risk factor for amyloidosis?

Amyloidosis is the name for a group of conditions caused by a build-up of amyloid protein deposits in organs and tissues throughout the body. A great many diseases can be classified as amyloidosis. The most well known are the cerebral amyloidoses Alzheimer's and Parkinson's disease. Lesser known are the systemic amyloidoses and Type-2-Diabetes. Although some genetic determinants have been identified, the large majority of patients suffering from amyloidosis have no identified family history, meaning the disease is sporadic and acquired. As symptoms in the early stages of the disease are often diffuse and mimic those of other conditions, diagnosis is... Read more →
Phase separation and protein aggregation

Phase separation and protein aggregation

Phase separation of biomolecules has recently been recognised as an important cellular process governing homogeneous organisation which is a driving force for cellular self-assembly. Multivalent interactions between biomolecules give rise to condensed phases with a spectrum of material properties from liquids to solids. The liquid-like properties (wetting, fusion, and dynamic exchange of internal components) of membraneless organelles such as P granules, stress granules, and the nucleolus have been demonstrated to be based on Liquid–liquid phase separation. The process of protein aggregation - disordered proteins which pathologically self-assemble into insoluble fibres that further aggregate into the plaques, tangles, or inclusions has... Read more →

Amytracker fluorescence spectra

We named our Amytracker molecules after their peak emission wavelength when they are bound to their target. That means, when Amytracker is bound to a target, it will emit fluorescence at peak emission indicated by the number associated with its name. To view the excitation and emission spectra, please select your Amytracker below : Amytracker 480 Amytracker 520 Amytracker 540 Amytracker 630 Amytracker 680 Excitation (blue lines) and emission (red lines) spectra of unbound Amytracker (dotted lines) and Amytracker bound to a target (solid lines). Read more →

Amytracker compared to Congo Red

Amytracker fluorescence is one order of magnitude brighter than Congo Red. The affinity of Amytracker is in the nM range and thus, Amytracker is typically used at several fold lower concentrations. In a comparative study using human amyloidosis tissue, Amytracker detected amyloid deposits in 15 % of Congo Red negative samples. While the pathological relevance of Congo Red negative deposits is currently unclear, Amytracker staining might give an indication of earlier states of disease. Unlike Congo Red, Amytracker does not bind to collagen or other cytoskeletal proteins. In the APP/PS1 and APP23 mouse models of Alzheimer's disease, Amytracker stains early... Read more →

Does Amytracker bind unspecifically?

We tested a wide range of human tissues and didn't observe unspecific staining in most cell types. Positive Amytracker staining was obtained in Paneth cell granules in the intestine stained and the binding target in these cells is yet unclear. Due to the high sensitivity of Amytracker towards amyloids, and its ability to detect Congo Red negative and non-thioflavinic assemblies, Amytracker might serve as an interesting tool to study functional amyloids in different species. Read More: Sjölander, D. et al. (2016) Establishing the fluorescent amyloid ligand h-FTAA for studying human tissues with systemic and localized amyloid. Amyloid Amyloid. 23(2), 98-108... Read more →

Fixation technique for Amytracker

Generally, we recommend light fixation using ice-cold ethanol or acetone. This is because formalin-fixation has been shown to reduce the ability to stain inclusion bodies. Otherwise there shouldn't be any issues. You can use paraffin sections or cryosections. Note that epitope exposure and antigen retrieval is not needed when applying Amytracker to paraffin embedded sections. Read More: Åslund, A. et al. (2009) Novel pentameric thiophene derivatives for in vitro and in vivo optical imaging of a plethora of protein aggregates in cerebral amyloidoses. ACS Chemical Biology, 4(8), 673-684. Read more →

Amytracker for use in various tissues and species

It is likely that Amytracker works on all kinds of tissues and species. Amytracker targets and detects the physical topography of the tertiary- and quaternary structure of mature and pre-fibrillar amyloid deposits. As such it is applicable to a wide range of animal models and different Amytracker molecules have been applied on tissue sections from humans, mice, cows, sheep, deer and Drosophila. Read more →

Amytracker binding

All Amytracker molecules are designed to interact with the same binding site on the amyloid oligomer. Competition assays have shown that Amytracker competes for the congo red binding site but show much higher affinity. In essence the binding cavity and binding mode of Amytracker is is dictated by a groove lined with repetitive positive charged side-chains. The detection of prefibrillar species appears dependent on 8 repetitive β sheets, composed of a minimum of eight in-register parallel-β-strands. Read More: Bäck, M. et al. (2016) Anionic Oligothiophenes Compete for Binding of X-34 but not PIB to Recombinant Aβ Amyloid Fibrils and Alzheimer's... Read more →

Amytracker for detection of Amyloidosis

Amytracker have been shown to bind with high affinity to aggregates composed of transthyretin (TTR) in Drosophila models of transthyretin amyloidosis (ATTR), as well as in human tissues The optotracers have been used to detect aggregates in following forms of human amyloid diseases: AA amyloidosis associated with accumulation of serum amyloid A (SAA) protein, isolated atrial amyloidosis associated with accumulation of atrial natriuretic factor, various forms of amyloid light chain (AL) amyloidosis and islet amyloid polypeptide (IAPP) or amylin which is believed to be of critical importance for the loss of β-cells in type 2 diabetes. Read More: Berg, I.... Read more →

Amytracker compared to Thioflavin

When Amytracker are not bound to a target, they exhibit an extremely low background fluorescence. Amytracker have also been shown to neither accelerate nor inhibit amyloid formation when used in recommended (substochoimetric) concentrations. Therefore, Amytracker are suitable for fibrillation assays and spectrophotometric detection. Amytracker have been shown to identify pre-fibrillar non-thioflavinophilic assemblies during in vitro fibrillation of Aβ peptides, insulin, lysozyme and prion protein with significantly reduced lag-phase compared to Thioflavin. Read More: Åslund, A. et al. (2009) Novel pentameric thiophene derivatives for in vitro and in vivo optical imaging of a plethora of protein aggregates in cerebral amyloidoses. ACS... Read more →

How should I dilute Amytracker?

We supply Amytracker molecules with high affinity toward amyloid proteins. For staining of cryo- or paraffin sections, diluting the supplied solutions 1:1000 should be sufficient. If you want to increase the intensity, you might increase the concentration and use 1:500 dilution instead. For live cell staining, we usually recommend to dilute our products 1:500. For fibrillation assays and spectroscopic application you should titrate the supplied optical tracer molecules, so you work with substochiometric amounts and make sure that there is not too much unbound probe in your sample. Read more →
Amyloids - the dark matter of biology

Amyloids - the dark matter of biology

Under some conditions, peptides or proteins may convert from their soluble forms into unsoluble highly ordered fibrillar aggregates. These aggregates may cause disease through various mechanisms. Prominent examples of aggregating peptides related to neurodegenerative diseases are Amyloid β peptides which play an important role in Alzheimer's disease and aggregating α-synuclein which is found in Lewy bodies that are a hallmark of Parkinson's disease and some forms of dementia. Multiple variants of systemic amyloidoses are caused by aggregating immunoglobin light chains, fragments of serum amyloid A protein or aggregating transthyretin. But many more forms of systemic and localized amyloid diseases exist.... Read more →
Amytracker for amyloid staining

Amytracker for amyloid staining

Amyloid detection has been notoriously difficult since current methods are either laborious, toxic and/or tend to detect mature fibrils but not protofibrils or premature aggregates. Amytracker are fluorescent tracer molecules binding to amyloids with high sensitivity. Amytracker have been shown to bind to prefibrillar states of amyloids and might therefore help to detect and investigate earlier pre-pathological states of amyloid diseases. As Amytracker are fluorescent only when bound to their target, they are well suited for fibrillation studies with much shorter lag phase and less background compared to other small molecule ligands. Amytracker are non-toxic and are well suited for... Read more →
Amytracker to investigate amyloid formation

Amytracker to investigate amyloid formation

The kinetics of amyloid formation from conformational conversion of a peptide or protein into its fibrillar form (amyloid) is studied using fibrillation assays using a spectrophotometer. This technique requires extremely low background fluorescence of the unbound probe and Thioflavin T has been widely used for this reason. The kinetic profile typically includes a lag phase that is followed by a rapid exponential growth phase and a plateau phase. As shown in the figure, Thioflavin T can reliably identify the presence of amyloid fibrils but are limited in detecting prefibrillar aggregates. Amytracker binds and detects prefibrillar aggregates present during the initial... Read more →
Amytracker for super-resolution microscopy

Amytracker for super-resolution microscopy

Super-resolution microscopy is becoming an important tool to study biological structures. As super-resolution techniques like STED overcome the physical diffraction limit of light, new microscopes with ever-decreasing resolution limits are being developed. Using these exciting techniques, the constraints are now imposed by the probes used for labelling. With STED microscopy, reaching a resolution of 20–40 nm, antibodies are no longer suitable as labelling probes since conjugated fluorophores will seem to be located far away from their target and spatial constraints will lead to spotty images. Due to their small size of less than 1 kDa and high affinity our fluorescent... Read more →
Amytracker for live cell Imaging

Amytracker for live cell Imaging

As functional aspects of amyloids as well as the dynamic processes involving amyloid formation and amyloid toxicity are of growing interest many researchers are interested to study these processes in living cells. Non-invasive techniques like fluorescence microsopy have been perfected in recent years for the study of living cells. Unfortunately, few non-toxic fluorescent dyes with high affinity to amyloids exist. Amytracker have been shown to readily pass membranes of living cells such as dorsal root ganglion cells and human pancreatic islet cells and bind intracellular protein aggregates. No cytotoxic effects have been observed even with high concentrations of Amytracker. For... Read more →
In vivo amyloid staining and intravital imaging

In vivo amyloid staining and intravital imaging

Intravital imaging is allowing researchers to capture images of biological processes in live animals. It has become an advanced tool to study the progression of Alzheimer's and other neurodegenerative diseases in transgenic mice. In vivo imaging using two-photon microscopy is an advantageous technique for observing tissues and organs at high resolution. Amytracker are suitable for in vivo studies since our probes are non-toxic, able to cross the blood-brain barrier and stain fibrillar deposits in animal models of amyloidogenic diseases. Presently, we supply Amytracker - Solid in sterile injection bottles optimized for labeling of protein aggregates in vivo for intravital imaging... Read more →

Characterisation of pathological protein aggregates at single molecule resolution

Ebba Biotech welcomes you to tune in to our webinar featuring Dr. Michael Morten from Imperial College London. During his talk titled "Characterisation of pathological protein aggregates at single-molecule resolution", Dr. Michael Morten will present his research using Amytracker. Dr. Michael Morten is a postdoctoral research associate in Yu Ye’s group at the Department of Brain Sciences, Imperial College London. His research focuses on developing imaging techniques to study protein aggregates using single-molecule localisation microscopy (SMLM). These methods are applied to image aggregates in a range of environments, including aggregates immobilised on coverslips, internalised in live and fixed cells, and... Read more →

Detection of functional amyloids in stress-treated mammalian cells

Ebba Biotech welcomes you to tune in to our webinar featuring Dr. Timothy Audas from Simon Fraser University. Dr. Audas will present his research using Amytracker to explore the detection of functional amyloids in stress-treated mammalian cells. Dr. Audas is an Associate Professor and Canada Research Chair at Simon Fraser University. In the Department of Molecular Biology and Biochemistry, his team studies stress response pathways that eukaryotic cells use to cope with harsh environmental conditions. Their primary focus is understanding the formation/function of natural amyloid aggregates, which share many biophysical characteristics with the toxic plaques and tangles that form in... Read more →

Amytracker - A New Frontier in Imaging of Amyloid Structures in Tissues

Ebba Biotech welcomes you to tune in to our webinar featuring Assistant Professor Oxana Klementieva from Lund's University. During her talk titled "Amytracker - A New Frontier in Imaging of Amyloid Structures in Tissues", Oxana Klementieva will detail her cutting-edge research into mechanisms of amyloid aggregation using novel imaging techniques. Read more about her work here: MMS Lab: https://mmslab.net/ Medical Microspectroscopy: https://www.lunduniversity.lu.se/luca... NanoLund: https://www.nano.lu.se/start About Oxana Klementieva I am an Associate Professor in the Department of Experimental Medicine at Lund University. I did my Ph.D. in 2012 in Barcelona and moved to Lund as a postdoc. In 2018, I established... Read more →

Amyloid fibril polymorphism in proteinopathies

Ebba Biotech's first webinar in 2023 is dedicated to "Amyloid Fibril Polymorphism" which has recently been shown to be a hallmark of many proteinopathies. One of the leading authorities in this field is Professor Per Hammarström from Linköping University. During this talk titled "Amyloid fibril polymorphism in proteinopathies", Prof. Hammarström discusses his work with protein misfolding in different amyloid diseases and various enhanced analytical methods pushing the boundaries within the amyloid field. Read more about his work using an Amytracker-like molecule for Advanced Imaging of amyloid aggregates here. Read more →

Consequences of coagulation in health and disease

Ebba Biotech welcomes you to listen to Prof. Resia Pretorius present her research findings using the Amytracker molecules. Her presentation titled “Consequences of coagulation in health and disease: The use of fluorescent markers” will detail past work with the Amytracker molecules within her group and her new exciting work with Long Covid patients. DISCLAIMER: Prof. Pretorius presentation is purely research based and for informational purposes only. This presentation contains no clinical advice for patients. If you have any health issues please contact your healthcare providers. Read more →

Optotracers - multifunctional fluorescent tracers

On the first of June 2021, Ferdinand Choong, Ebba Biotech's co-founder, and Assistant Professor at Karolinska Institutet and AIMES (Center for the Advancement of Integrated Medical and Engineering), presented his research using Ebba Biotech's optotracers at the digital event Lab & Diagnostics of the Future 2021, held by Life Science Sweden. At this event, Ferdinand spoke about Ebba Biotech's optotracers multifunctional tracer for disease research and diagnostics. He explains the technical concept in large and Ebba Biotech's three product series, Amytracker - used to detect amyloids and other protein aggregates, Ebba Biolight - used to detect bacteria and biofilm, Carbotrace... Read more →

Fluorescence microscopy techniques using Amytracker-like molecules

A paper in the scientific video journal Jove (Nyström et al. (2017) Jove 128, 1–7) describes the application of Amytracker-like Molecules in combination with fluorescence microscopy techniques for detection and exploration of protein aggregates. Read more →

Peter Nilsson develops multifunctional tools for diagnosis and therapy

Peter Nilson has been elected as future research leader from the Swedish Foundation for Strategic Research (SSF). His work about the development of multifunctional tools for diagnosis and therapy has led to the development of our Amytracker molecules. Read more →