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
收藏
页码：200 / 204
页数：5
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