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

  • Rodríguez-Rodríguez C
  • Rimola A
  • Rodríguez-Santiago L
 et al. 
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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.

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