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.
2010
46
7
1156
1158
http://pubs.rsc.org/en/content/articlelanding/2010/cc/b912396b
tioflavine; amyloid
R. Rodriguez-Rodriguez; A. Rimola; L. Rodriguez-Santiago; P. Ugliengo; A. Alvarez-Larena; H. Gutierrez-de-Teran; M. Sodupe; P. Gonzalez-Duarte...espandi
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2318/130857
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