Crystal structure of thioflavin-T and its binding to amyloid fibrils: insights at the molecular level.
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.
Rodríguez-Rodríguez
Cristina
C
Departament de Química, Universitat Autònoma de Barcelona, 08193 Bellaterra, Barcelona, Spain.
Rimola
Albert
A
Rodríguez-Santiago
Luis
L
Ugliengo
Piero
P
Alvarez-Larena
Angel
A
Gutiérrez-de-Terán
Hugo
H
Sodupe
Mariona
M
González-Duarte
Pilar
P
D016229:Amyloid beta-Peptides / Q000737:chemistry*; D052160:Benzothiazoles; D001665:Binding Sites; D018360:Crystallography, X-Ray; D005456:Fluorescent Dyes / Q000737:chemistry; D008968:Molecular Conformation; D010446:Peptide Fragments / Q000737:chemistry*; D011485:Protein Binding; D017433:Protein Structure, Secondary; D013844:Thiazoles / Q000737:chemistry*
D016229:Amyloid beta-Peptides; D052160:Benzothiazoles; D005456:Fluorescent Dyes; D010446:Peptide Fragments; D013844:Thiazoles; C075222:amyloid beta-protein (1-42); C009462:thioflavin T