Combining X-ray data on thioflavin-T and theoretical calculations on its binding to a peptide model for Aβ1–42 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.
Crystal structure of thioflavin-T and its binding to amyloid fibrils: insights at the molecular level
UGLIENGO, Piero;
2010-01-01
Abstract
Combining X-ray data on thioflavin-T and theoretical calculations on its binding to a peptide model for Aβ1–42 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.
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