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

Cristina Rodríguez-Rodríguez, Albert Rimola, Luis Rodríguez-Santiago, Piero Ugliengo, Ángel Álvarez-Larena, Hugo Gutiérrez-De-Terán, Mariona Sodupe, Pilar González-Duarte

Producció científica: Contribució a revistaArticleRecercaAvaluat per experts

83 Cites (Scopus)

Resum

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 The Royal Society of Chemistry.
Idioma originalAnglès
Pàgines (de-a)1156-1158
RevistaChemical Communications
Volum46
Número7
DOIs
Estat de la publicacióPublicada - 15 de febr. 2010

Fingerprint

Navegar pels temes de recerca de 'Crystal structure of thioflavin-T and its binding to amyloid fibrils: Insights at the molecular level'. Junts formen un fingerprint únic.

Com citar-ho