Crystal structure of thioflavin-T and its binding to amyloid fibrils: insights at the molecular level.
Chem Commun (Camb)
; 46(7): 1156-8, 2010 Feb 21.
Article
en En
| MEDLINE
| ID: mdl-20126745
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.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Fragmentos de Péptidos
/
Tiazoles
/
Péptidos beta-Amiloides
Idioma:
En
Revista:
Chem Commun (Camb)
Asunto de la revista:
QUIMICA
Año:
2010
Tipo del documento:
Article
País de afiliación:
España