Fluorescence Spectroscopy Study on the Interaction between Evodiamine and Bovine Serum Albumin

被引：32

作者：

Tan, Mingxiong ^{[1
,2
]}

Liang, Weijiang ^{[1
]}

Luo, Xujian ^{[1
]}

Gu, Yunqiong ^{[1
]}

机构：

[1] Yulin Normal Univ, Sch Chem & Mat, Yulin 537000, Peoples R China

[2] Guangxi Normal Univ, Sch Chem & Chem Engn, Key Lab Chem & Mol Engn Med Resources, Guilin 541004, Peoples R China

来源：

JOURNAL OF CHEMISTRY | 2013年 / 2013卷

基金：

中国国家自然科学基金;

关键词：

BINDING; DERIVATIVES; COMPLEXES;

D O I：

10.1155/2013/308054

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

The interaction of evodiamine (Evo) with bovine serum albumins (BSAs) at different two temperatures (298 and 310 K) was investigated by means of fluorescence spectroscopy. The experimental results showed that Evo binds with BSA via a static quenching procedure with association constants K of 1.61 x 10(6) L/mol at 298 K and 6.78 x 10(5) L/mol at 310 K. The number of bound Evo molecules per protein is 1.31 at 298 K and 1.33 at 310 K. The results suggested that Evo reacts with BSA chiefly through hydrophobic and electrostatic interactions, and it does not alter the alpha-helical nature of BAS.

引用

页数：6

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