https://scholars.lib.ntu.edu.tw/handle/123456789/406719
標題: | Effect of guanidine hydrochloride and urea on the interaction of 6-thioguanine with human serum albumin: a spectroscopic and molecular dynamics based study | 作者: | Ishtikhar M. Khan A. Chang C.-K. Lin L.T.-W. Wang S.S.S. Khan R.H. |
關鍵字: | 6-thioguanine;circular dichroism;fluorescence spectroscopy;guanidine hydrochloride denaturation;human serum albumin;molecular dynamics;urea denaturation | 公開日期: | 2016 | 卷: | 34 | 期: | 7 | 起(迄)頁: | 1409-1420 | 來源出版物: | Journal of Biomolecular Structure and Dynamics | 摘要: | 6-thioguanine (6-TG) is an antineoplastic, nucleobase guanine, purine analog drug belongs to thiopurine drug-family of antimetabolites. In the present study, we report an experimental approach towards interaction mechanism of 6-TG with human serum albumin (HSA) and examine the chemical stability of HSA in the presence of denaturants such as guanidine hydrochloride (GdnHCl) and urea. Interaction of 6-TG with HSA has been studied by various spectroscopic and spectropolarimeteric methods to investigate what short of binding occurs at physiological conditions. 6-TG binds in the hydrophobic cavity of subdomain IIA of HSA by static quenching mechanism which induces conformation alteration in the protein structure. That helpful for further study of denaturation process where change in secondary structures causes unfolding of protein that also responsible for severance of domain III from rest of the protein part. We have also performed molecular simulation and molecular docking study in the presence of denaturating agents to determine the binding property of 6-TG and the effect of denaturating agents on the structural activity of HSA. We had found that GdnHCl is more effective denaturating agent when compared to urea. Hence, this study provides straight evidence of the binding mechanism of 6-TG with HSA and the formation of intermediate or unfolding transition that causes unfolding of HSA. ? 2016 Informa UK Limited, trading as Taylor & Francis Group. |
URI: | https://scholars.lib.ntu.edu.tw/handle/123456789/406719 | ISSN: | 07391102 | DOI: | 10.1080/07391102.2015.1054433 |
顯示於: | 化學工程學系 |
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