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

Chem Commun (Camb). 2010 Feb 21;46(7):1156-8. doi: 10.1039/b912396b. Epub 2010 Jan 4.

Abstract

Combining X-ray data on thioflavin-T and theoretical calculations on its binding to a peptide model for Abeta(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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amyloid beta-Peptides / chemistry*
  • Benzothiazoles
  • Binding Sites
  • Crystallography, X-Ray
  • Fluorescent Dyes / chemistry
  • Molecular Conformation
  • Peptide Fragments / chemistry*
  • Protein Binding
  • Protein Structure, Secondary
  • Thiazoles / chemistry*

Substances

  • Amyloid beta-Peptides
  • Benzothiazoles
  • Fluorescent Dyes
  • Peptide Fragments
  • Thiazoles
  • amyloid beta-protein (1-42)
  • thioflavin T