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
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Research Support, Non-U.S. Gov't
MeSH terms
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Amyloid beta-Peptides / chemistry*
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Benzothiazoles
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Binding Sites
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Crystallography, X-Ray
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Fluorescent Dyes / chemistry
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Molecular Conformation
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Peptide Fragments / chemistry*
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Protein Binding
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Protein Structure, Secondary
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Thiazoles / chemistry*
Substances
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Amyloid beta-Peptides
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Benzothiazoles
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Fluorescent Dyes
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Peptide Fragments
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Thiazoles
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amyloid beta-protein (1-42)
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thioflavin T