期刊
SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY
卷 74, 期 4, 页码 964-971出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.saa.2009.09.001
关键词
8-Bromoadenosine; Human serum albumin (HSA); Fluorescence spectra; Synchronous fluorescence; Molecular modeling; Determination
类别
资金
- Nature Science Foundation of China [20673034, 20772024]
- Chinese Ministry of Education [20060476001]
- Department of Education of Henan Province [2006150012]
This study was designed to examine the interaction of 8-bromoadenosine with human serum albumin (HSA) by fluorescence spectroscopy in combination with molecular modeling under simulative physiological conditions The results Of fluorescence measurements indicate that 8-bromoadenosine has a strong ability to quench the intrinsic fluorescence of HSA through static quenching procedure The binding constants (K) at different temperatures and thermodynamic parameters, enthalpy changes (Delta H) and entropy changes (Delta S) were calculated according to the fluorescence data The results showed that the hydrophobic force played the major role in the binding of 8-bromoadenosine to HSA The fluorescence experimental results were in agreement with the results obtained by molecular modeling study The effects of some normal positive and negative ions on the binding constants were also discussed Moreover, the synchronous fluorescence technique was used to characterize the interaction of 8-bromoadenosine to HSA and successfully applied to determine the total proteins in human serum, urine and saliva samples at room temperature under the optimum conditions with a wide linear range and satisfactory results (C) 2009 Elsevier B.V. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据