ArticleACS chemical neuroscience2015
Fluorescent filter-trap assay for amyloid fibril formation kinetics in complex solutions.
Article in ACS chemical neuroscience, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Article
- A Palette of Fluorescent AInternational journal of molecular sciences · 2022Article
- Expression of N-Terminal Cysteine AβBiochemistry · 2021Article
- Quantifying misfolded protein oligomers as drug targets and biomarkers in Alzheimer and Parkinson diseases.Nature reviews. Chemistry · 2021Review
- Kinetic fingerprints differentiate the mechanisms of action of anti-Aβ antibodies.Nature structural & molecular biology · 2020Article
- Dynamics of oligomer populations formed during the aggregation of Alzheimer's Aβ42 peptide.Nature chemistry · 2020Article
- Heterologous Expression of Immature Forms of Human Islet Amyloid Polypeptide in Yeast Triggers Intracellular Aggregation and Cytotoxicity.Frontiers in microbiology · 2020Article
- Evaluation of the photo-degradation of Alzheimer's amyloid fibrils with a label-free approach.Chemical communications (Cambridge, England) · 2018Article
- Neuroprotective effect of ipriflavone against scopolamine-induced memory impairment in rats.Psychopharmacology · 2017Article
- The small heat shock proteins αB-crystallin (HSPB5) and Hsp27 (HSPB1) inhibit the intracellular aggregation of α-synuclein.Cell stress & chaperones · 2017Article
- Direct High Affinity Interaction between Aβ42 and GSK3α Stimulates Hyperphosphorylation of Tau. A New Molecular Link in Alzheimer's Disease?ACS chemical neuroscience · 2016Article
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amyloid fibrils are the most distinct components of the plaques associated with various neurodegenerative diseases. Kinetic studies of amyloid fibril formation shed light on the microscopic mechanisms that underlie this process as well as the contributions of internal and external factors to the interplay between different mechanistic steps. Thioflavin T is a widely used noncovalent fluorescent probe for monitoring amyloid fibril formation; however, it may suffer from limitations due to the unspecific interactions between the dye and the additives. Here, we present the results of a filter-trap assay combined with the detection of fluorescently labeled amyloid β (Aβ) peptide. The filter-trap assay separates formed aggregates based on size, and the fluorescent label attached to Aβ allows for their detection. The times of half completion of the process (t1/2) obtained by the filter-trap assay are comparable to values from the ThT assay. High concentrations of human serum albumin (HSA) and carboxyl-modified polystyrene nanoparticles lead to an elevated ThT signal, masking a possible fibril formation event. The filter-trap assay allows fibril formation to be studied in the presence of those substances and shows that Aβ fibril formation is kinetically inhibited by HSA and that the amount of fibrils formed are reduced. In contrast, nanoparticles exhibit a dual-behavior governed by their concentration.
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