Interaction of two flavonols with fat mass and obesity-associated protein investigated by fluorescence quenching and molecular docking.
J Biomol Struct Dyn
; 36(13): 3388-3397, 2018 Oct.
Article
em En
| MEDLINE
| ID: mdl-28978264
ABSTRACT
The binding of two flavonols with fat mass and obesity-associated protein (FTO) was studied using fluorescence spectroscopy, Stern-Volmer kinetics, UV-Vis absorption, and molecular docking. The quenching of FTO fluorescence was determined to be static with binding constants on the order of 104 M-1. The interaction was studied over three temperatures, and the binding was found to be exothermic with a positive change in entropy. Thermodynamic analysis and molecular modeling suggest that hydrophobic interaction and hydrogen bonding interaction are the main binding force in stabilizing the flavonol-FTO complex.
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Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Flavonóis
/
Interações Hidrofóbicas e Hidrofílicas
/
Dioxigenase FTO Dependente de alfa-Cetoglutarato
Tipo de estudo:
Risk_factors_studies
Idioma:
En
Revista:
J Biomol Struct Dyn
Ano de publicação:
2018
Tipo de documento:
Article
País de afiliação:
China