Investigation of binding properties of dicationic styrylimidazo[1,2-a]pyridinium dyes to human serum albumin by spectroscopic techniques.
Luminescence
; 32(1): 86-92, 2017 Feb.
Article
en En
| MEDLINE
| ID: mdl-27121543
ABSTRACT
The binding interaction between two dicationic styrylimidazo[1,2-a]pyridinium dyes and human serum albumin (HSA) was investigated at physiological conditions using fluorescence, UV-vis absorption, and circular dichroism (CD) spectroscopies. Analysis of the fluorescence titration data at different temperatures suggested that the fluorescence quenching mechanism of HSA by these dyes was static. The calculated thermodynamic parameters (ΔG°, ΔH° and ΔS°) indicated that hydrogen bonding and van der Waals forces played a major role in the formation of the dye-HSA complex. Binding distances (r) between dyes and HSA were calculated according to Förster's non-radiative energy transfer theory. Studies of conformational changes of HSA using CD measurements indicate that the α-helical content of the protein decreased upon binding of the dyes. Copyright © 2016 John Wiley & Sons, Ltd.
Palabras clave
Texto completo:
1
Base de datos:
MEDLINE
Asunto principal:
Compuestos de Piridinio
/
Albúmina Sérica
/
Colorantes Fluorescentes
/
Imidazoles
Límite:
Humans
Idioma:
En
Revista:
Luminescence
Asunto de la revista:
BIOFISICA
/
BIOQUIMICA
Año:
2017
Tipo del documento:
Article
País de afiliación:
Turquía