ArticlePrion2020
Effect of the fluorescent probes ThT and ANS on the mature amyloid fibrils.
Article in Prion, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 94 citations in OpenAlex.
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- Unraveling the structure-activity relationships of organometallic ferrocene-pyrazole and ferrocene-pyrimidine curcumin analogues in amyloid-β aggregation and glioblastoma treatment.Scientific reports · 2025Article
- Combating multiple aetiologies of Alzheimer's disease to rescue behavioural deficits.Chemical science · 2025Article
- Protective Effect of a Hexapeptide Derived from Rotifer-Specific SCO-Spondin Against Beta-Amyloid Toxicity.International journal of molecular sciences · 2025Article
- L-tyrosine inhibits the formation of amyloid fibers of human lysozyme at physiological pH and temperature.Amino acids · 2025Article
- Engineered Protein Fibers with Reinforced Mechanical Properties Via β-Sheet High-Order Assembly.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Analysis of Amyloid Fibrillation of Two Family 1 Glycoside Hydrolases.International journal of molecular sciences · 2024Article
- Modulation of Alzheimer's Disease Aβ40 Fibril Polymorphism by the Small Heat Shock Protein αB-Crystallin.Journal of the American Chemical Society · 2024Article
- Formulation and Characterization of Silibinin Entrapped Nano-Liquid Crystals for Activity against AβAAPS PharmSciTech · 2024Article
- Amyloid-β Oligomer-Induced Electrophysiological Mechanisms and Electrical Impedance Changes in Neurons.Sensors (Basel, Switzerland) · 2024Article
- Investigation of the Effect of Pyrogallol on the Formation of Amylin Amyloid Fibrils as a Strategy for the Treatment of Type 2 Diabetic Patients: A Theoretical and Experimental Study.Journal of fluorescence · 2024Article
- Carboxylic Group Functionalized Carbon Quantum Dots inhibit Hen Egg White Lysozyme Amyloidogenesis, leading to the Formation of Spherical Aggregates with Reduced Toxicity and ROS Generation.Current protein & peptide science · 2024Article
- Recent Developments of Hybrid Fluorescence Techniques: Advances in Amyloid Detection Methods.Current protein & peptide science · 2024Review
- Widespread amyloid aggregates formation by Zika virus proteins and peptides.Protein science : a publication of the Protein Society · 2023Article
- Only kosmotrope anions trigger fibrillization of the recombinant core spidroin eADF4(C16) from Araneus diadematus.Protein science : a publication of the Protein Society · 2023Article
- Amine Group Surface-Functionalized Carbon Quantum Dots Exhibit Anti-amyloidogenic Effects Towards Hen Egg White Lysozyme by Inducing Formation of Nontoxic Spherical Aggregates.The protein journal · 2023Article
- Global analysis of kinetics reveals the role of secondary nucleation in recombinant spider silk self-assembly.Protein science : a publication of the Protein Society · 2023Article
- Amyloidogenic proteins in the SARS-CoV and SARS-CoV-2 proteomes.Nature communications · 2023Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Fluorescent probes thioflavin T (ThT) and 1-anilino-8-naphthalene sulfonate (ANS) are widely used to study amyloid fibrils that accumulate in the body of patients with serious diseases, such as Alzheimer's, Parkinson's, prion diseases, etc. However, the possible effect of these probes on amyloid fibrils is not well understood. In this work, we investigated the photophysical characteristics, structure, and morphology of mature amyloid fibrils formed from two model proteins, insulin and lysozyme, in the presence of ThT and ANS. It turned out that ANS affects the secondary structure of amyloids (shown for fibrils formed from insulin and lysozyme) and their fibers clusterization (valid for lysozyme fibrils), while ThT has no such effects. These results confirm the differences in the mechanisms of these dyes interaction with amyloid fibrils. Observed effect of ANS was explained by the electrostatic interactions between the dye molecule and cationic groups of amyloid-forming proteins (unlike hydrophobic binding of ThT) that induce amyloids conformational changes. This interaction leads to weakening repulsion between positive charges of amyloid fibrils and can promote their clusterization. It was shown that when fibrillogenesis conditions and, consequently, fibrils structure is changing, as well as during defragmentation of amyloids by ultrasonication, the influence of ANS to amyloids does not change, which indicates the universality of the detected effects. Based on the obtained results, it was concluded that ANS should be used cautiously for the study of amyloid fibrils, since this fluorescence probe have a direct effect on the object of study.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.