Study on the binding of Thioflavin T to β-sheet-rich and non- β-sheet cavities

摘要: Abstract Amyloid fibril formation plays a role in more than 20 diseases including Alzheimer’s disease. In vitro detection of these fibrils is often performed using Thioflavin T (ThT), though the ThT binding mode largely unknown. present study, spectral properties environments representing β-sheet-rich and non-β-sheet cavities were examined. Acetylcholinesterase γ-cyclodextrin induced characteristic fluorescence similar to that with amyloid fibrils, whereas β-cyclodextrin transthyretin did not. The acetylcholinesterase diameter only could accommodate two ions according molecular modelling. Binding stoichiometry studies also showed possible ions. Thus, 8–9 A length able entire ion. importance cavity capable ions, among others, indicates an excimer plausible mechanism for fluorescence. We propose where appropriate size running parallel axis have previously been proposed several models.