Application of molecular modelling and spectroscopic approaches for investigating the binding of tanshinone IIA to human serum albumin

被引：10

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：

JOURNAL OF CHEMICAL THERMODYNAMICS | 2013年 / 58卷

基金：

中国国家自然科学基金;

关键词：

Molecular modelling; Tanshinone IIA; Human serum albumin; Fluorescence quenching technology; FT-IR spectroscopy; Circular dichroism; SALVIA-MILTIORRHIZA; FLUORESCENCE; DERIVATIVES; WARFARIN; WATER; SITE;

D O I：

10.1016/j.jct.2012.11.009

中图分类号：

O414.1 [热力学];

学科分类号：

070201 [理论物理];

摘要：

The interaction of tanshinone IIA and human serum albumin (HSA) has been characterised by molecular modelling, fluorescence, Fourier transform infrared (FT-IR) and circular dichroism (CD) spectroscopic methods. The results of molecular modelling suggested that tanshinone IIA located within the binding pocket of subdomain IIA of HSA is held mainly by hydrophobic forces. Fluorescence titration revealed that tanshinone IIA could quench the intrinsic fluorescence of HSA. The binding constants at three temperatures (296, 303, and 310) K are (6.42 . 10(4), 1.54 . 10(5), and 4.35 . 10(5)) dm(3) . mol(-1), respectively. In addition, the studies of CD spectroscopy and FT-IR spectroscopy showed that the binding of tanshinone IIA to HSA changed molecular conformation of HSA. (C) 2012 Elsevier Ltd. All rights reserved.

引用

页码：206 / 210

页数：5

共 35 条

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Investigation of the interaction between trazodone hydrochloride and bovine serum albumin [J].