Molecular spectroscopic on interaction between Methyl hesperidin and Buman serum albumin

被引：9

作者：

Li, Jinhua ^{[1
]}

Wang, Sumin ^{[1
]}

机构：

[1] Xian Technol Univ, Sch Mat & Chem Engn, Xian 710032, Peoples R China

来源：

SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY | 2013年 / 102卷

基金：

中国国家自然科学基金;

关键词：

Methyl hesperidin; Buman serum albumin; Fluorescence quenching technology; UV absorbance spectra; FT-IR spectroscopy; FLUORESCENCE; BINDING; DERIVATIVES; FLAVONOIDS; PROTEINS; ACID;

D O I：

10.1016/j.saa.2012.10.012

中图分类号：

O433 [光谱学];

学科分类号：

0703 ; 070302 ;

摘要：

The interaction of Methyl hesperidin (MH) with Buman serum albumin was studied by spectroscopic methods including Fluorescence quenching technology, UV absorbance spectra and Fourier transform infrared (FT-IR) spectroscopy under simulative physiological conditions. The result of fluorescence titration revealed that Methyl hesperidin could quench the intrinsic fluorescence of BSA and the quenching mechanism should be a combined quenching process. The binding constants at three temperatures (296, 303, and 310 K) were 1.82, 2.69, and 3.4 x 10(4) L mol(-1), respectively. The distance between donor (BSA) and acceptor (MH) was 5.54 nm according to the Forster theory of non-radiation energy transfer. In addition, FT-IR spectroscopy showed that the binding of MH to BSA changed the secondary structure of protein. 2012 Elsevier B.V. All rights reserved.

引用

页码：200 / 204

页数：5

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