Journal
CHEMICAL COMMUNICATIONS
Volume 46, Issue 7, Pages 1156-1158Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/b912396b
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Funding
- MICINN [CTQ2008-06381/BQU]
- DURSI [SGR2009-68, SGR2009-638]
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Combining X-ray data on thioflavin-T and theoretical calculations on its binding to a peptide model for A beta(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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