Crystal structure of thioflavin-T and its binding to amyloid fibrils: insights at the molecular level

Abstract

Combining X-ray data on thioflavin-T and theoretical calculations on its binding to a peptide model for Aβ_1–42 fibrils gives evidence of main stabilizing interactions, which influence the dihedral angle between the two moieties of thioflavin-T and thereby its fluorescence properties; these results shed new light on possible strategies for the design of dyes to bind amyloid fibrils more specifically.