Study on the interaction of 6-thioguanine with bovine serum albumin by spectroscopic techniques

被引：41
|
作者：
Qu, Peng [1 ]
Lu, Hua [1 ]
Ding, Xiaoyu [1 ]
Tao, Yi [1 ]
Lu, Zuhong [1 ]
机构：
[1] Southeast Univ, State Key Lab Bioelect, Sch Biol Sci & Med Engn, Nanjing 210096, Peoples R China
来源：
JOURNAL OF MOLECULAR STRUCTURE | 2009年 / 920卷 / 1-3期
基金：
中国国家自然科学基金;
关键词：
6-Thioguanine; Bovine serum albumin; UV-Vis absorption; Florescence spectroscopy; CD spectra; FLUORESCENCE SPECTROSCOPY; PROTEIN; 6-MERCAPTOPURINE; BILIRUBIN; MECHANISM; ELECTRODE; DISEASE; COMPLEX; ACID;
D O I：
10.1016/j.molstruc.2008.10.041
中图分类号：
O64 [物理化学（理论化学）、化学物理学];
学科分类号：
070304 ; 081704 ;
摘要：
The interaction of 6-thioguanine (6-TG) and bovine serum albumin (BSA) was investigated by UV-Vis absorption, circular dichroism (CD) spectra and florescence spectroscopy. The experimental results indicated that the quenching mechanism of BSA by 6-TG was a static quenching procedure. Various binding parameters have been evaluated. Delta H-0, Delta G(0) and Delta S-0, indicated that hydrophobic forces played a major role when 6-TG interacted with BSA. Based on the Forster's theory of non-radiation energy transfer, the binding distance, r between the donor (BSA) and acceptor (6-TG) was evaluated. CD spectral results showed that the binding of 6-TG to BSA induced conformational changes in BSA. (C) 2008 Elsevier B.V. All rights reserved.
引用
收藏
页码：172 / 177
页数：6
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