Spectroscopic investigation of interaction between mangiferin and bovine serum albumin

被引：117

作者：

Lin, Hui ^{[1
]}

Lan, Jingfeng ^{[1
]}

Guan, Min ^{[1
]}

Sheng, Fenling ^{[1
]}

Zhang, Haixia ^{[1
]}

机构：

[1] Lanzhou Univ, Coll Chem & Chem Engn, Lanzhou 730000, Peoples R China

来源：

SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY | 2009年 / 73卷 / 05期

基金：

中国国家自然科学基金;

关键词：

Mangiferin; Bovine serum albumin; Fluorescence; Fourier transform infrared spectroscopy; MOLECULAR MODELING METHODS; NATURALLY-OCCURRING GLUCOSYLXANTHONE; ANEMARRHENA-ASPHODELOIDES; FLUORESCENCE SPECTROSCOPY; OPTICAL SPECTROSCOPY; BINDING; CONSTITUENTS; ISOFRAXIDIN; MEMBRANES; OXYGEN;

D O I：

10.1016/j.saa.2009.04.025

中图分类号：

O433 [光谱学];

学科分类号：

0703 ; 070302 ;

摘要：

The mechanism of interaction between mangiferin (MA) and bovine serum albumin (BSA) in aqueous solution was investigated by fluorescence spectra, synchronous fluorescence spectra, absorbance spectra and Fourier transform infrared (FT-IR) spectroscopy. The binding constants and binding sites of MA to BSA at different reaction times were calculated. And the distance between MA and BSA was estimated to be 5.20 nm based on Foster's theory. In addition, synchronous fluorescence and FT-IR measurements revealed that the secondary structures of the protein changed after the interaction of MA with BSA. As a conclusion, the interaction between the anti-diabetes Chinese medicine MA and BSA may provide some significant information for the mechanism of the traditional chinese medicine MA on the protein level to cure diabetes or other diseases. (C) 2009 Elsevier B.V. All rights reserved.

引用

页码：936 / 941

页数：6

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