Investigation of nitroxoline-human serum albumin interactions by spectroscopic methods

被引：9

作者：

Zhang WanJu ^{[1
,2
,3
]}

Xiong XuJie ^{[1
]}

Wang Fang ^{[1
]}

Li Li ^{[1
]}

Zhang Yan ^{[1
]}

Xiao WenPing ^{[1
]}

Liu Yi ^{[2
,3
]}

机构：

[1] Huanggang Normal Univ, Hubei Key Lab Proc & Applicat Catalyt Mat, Huanggang 438000, Peoples R China

[2] Wuhan Univ, Coll Chem & Mol Sci, Minist Educ, State Key Lab Virol, Wuhan 430072, Peoples R China

[3] Wuhan Univ, Coll Chem & Mol Sci, Minist Educ, Key Lab Analyt Chem Biol & Med, Wuhan 430072, Peoples R China

来源：

SCIENCE CHINA-CHEMISTRY | 2014年 / 57卷 / 12期

基金：

中国国家自然科学基金;

关键词：

nitroxoline; human serum albumin; spectroscopic methods; interaction; BINDING; FORCES;

D O I：

10.1007/s11426-014-5230-8

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Nitroxoline is a wide spectrum antibacterial and is one of the most important urinary antiseptics. The interaction between nitroxoline and human serum albumin (HSA) has been investigated systematically by fluorescence spectroscopy, synchronous fluorescence, three-dimensional fluorescence, CD spectroscopy and UV-Vis absorption spectroscopy. The results indicated that the quenching of HSA by nitroxoline was static. The corresponding thermodynamic parameters Delta H, Delta S and Delta G calculated according to van't Hoff equation revealed that the intermolecular forces acting between nitroxoline and HSA were mainly hydrogen bonding and van der Waals forces. The conformational changes in the interaction were studied by synchronous fluorescence, CD spectroscopy and three-dimensional fluorescence spectra which showed changes in the microenvironment and conformation of HSA.

引用

页码：1690 / 1695

页数：6

共 22 条

[1] THE BINDING INTERACTION OF COOMASSIE BLUE WITH PROTEINS [J].