Spectroscopic study on interaction of quercitrin with human serum albumin / 中草药
Chinese Traditional and Herbal Drugs
;
(24): 676-679, 2011.
Artigo
em Chinês
| WPRIM
| ID: wpr-855623
ABSTRACT
Objective:
To study the interaction of quercitrin with human serum albumin (HSA) and the influence of glucose.Methods:
To investigate the interaction mechanism between quercitrin and HSA by spectroscopic method; to calculate the binding constants, binding sites, and binding distance according to double logarithmic plot and Föster's energy transfer theory, respectively; to explain the type of interaction force between quercitrin with HSA by thermodynamic parameters; to discuss the conformation change of HSA via synchronous fluorescence spectra.Results:
The fluorescence quenching mechanism of quercitrin to HSA was static quenching; The binding constants and the number of binding sites decreased with the increasing of temperature and glucose; The distance between the donor and acceptor was less than 7 nm; The hydrophobic forces played a major role in stabilizing quercetrin and HSA complex; The binding reaction had changed the micro-environmention of tryptophan residues.Conclusion:
Quercetrin could bind with HSA and change the conformation of HSA; The physiological concentration of glucose increases the binding constants and the number of binding sites of quercetrin with HSA.
Texto completo:
DisponíveL
Índice:
WPRIM (Pacífico Ocidental)
Idioma:
Chinês
Revista:
Chinese Traditional and Herbal Drugs
Ano de publicação:
2011
Tipo de documento:
Artigo
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