中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
Investigation on the interaction between a heterocyclic aminal derivative, sbdc, and human serum albumin

文献类型:期刊论文

作者Zhou, Qiuju1,2; Xiang, Junfeng1; Tang, Yalin1; Liao, Jiangpeng2,3; Yu, Chuyi3; Zhang, Hong1; Li, Lin1; Yang, Yueyang1; Xu, Guangzhi1
刊名Colloids and surfaces b-biointerfaces
出版日期2008-01-15
卷号61期号:1页码:75-80
关键词Heterocyclic ketene aminals Human serum albumin Fluorescence quenching Circular dichroism Protein-ligand docking
ISSN号0927-7765
DOI10.1016/j.colsurfb.2007.07.007
通讯作者Tang, yalin(tangyl@iccas.ac.cn)
英文摘要The interaction between a novel promising drug (spiro[(2r,3r,4s)-4-benzyloxy-2,3-isopropylidene-dioxy-1-oxa-cyclopentane-5,5'-(2-benzoylmethylene-1,3-diaza-cyclohexane)] (sbdc)) and human serum albumin (hsa) under physiological conditions has been investigated by using fluorescence, absorption, and circular dichroism (cd) spectroscopic techniques in combination with protein-ligand docking study. it was observed that sbdc has a strong ability to quench the intrinsic fluorescence of hsa through a static quenching procedure. the association constants of sbdc with hsa were determined at different temperatures based on fluorescence quenching results. the negative delta h and positive delta s values in case of sbdc-hsa complex showed that apart from an initial hydrophobic association, both van der waals interactions and hydrogen bonding play a vital role in the binding of sbdc to hsa. the quantitative analysis data of cd spectra showed that the binding of sbdc to hsa induced conformational changes in hsa and the alpha-helix of 52.1% in free hsa increased to 55.7% in hsa-sbdc complex. the distance between donor (hsa) and acceptor (sbdc) was obtained according to the forster's theory of non-radiation energy transfer. data obtained by spectroscopic techniques and protein-ligand docking study suggested that sbdc binds to residues located in subdomain iia of hsa. (c) 2007 elsevier b.v. all rights reserved.
WOS关键词KETENE AMINALS ; FUSED DIAZAHETEROCYCLES ; ETHYL BROMOACETATE ; OCHRATOXIN-A ; BINDING-SITE ; FLUORESCENCE ; PROTEIN ; CYCLOCONDENSATION ; ALKYLATION ; ROUTE
WOS研究方向Biophysics ; Chemistry ; Materials Science
WOS类目Biophysics ; Chemistry, Physical ; Materials Science, Biomaterials
语种英语
WOS记录号WOS:000252584300011
出版者ELSEVIER SCIENCE BV
URI标识http://www.irgrid.ac.cn/handle/1471x/2392824
专题中国科学院大学
通讯作者Tang, Yalin
作者单位1.Chinese Acad Sci, Inst Chem, Beijing Natl Lab Mol Sci BNLMS, Ctr Mol Sci,State Key Lab Struct Chem Unstable &, Beijing 100080, Peoples R China
2.Chinese Acad Sci, Grad Sch, Beijing 100080, Peoples R China
3.Chinese Acad Sci, Inst Chem, Lab Mol Recognit & Select Synth, Beijing 100080, Peoples R China
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GB/T 7714
Zhou, Qiuju,Xiang, Junfeng,Tang, Yalin,et al. Investigation on the interaction between a heterocyclic aminal derivative, sbdc, and human serum albumin[J]. Colloids and surfaces b-biointerfaces,2008,61(1):75-80.
APA Zhou, Qiuju.,Xiang, Junfeng.,Tang, Yalin.,Liao, Jiangpeng.,Yu, Chuyi.,...&Xu, Guangzhi.(2008).Investigation on the interaction between a heterocyclic aminal derivative, sbdc, and human serum albumin.Colloids and surfaces b-biointerfaces,61(1),75-80.
MLA Zhou, Qiuju,et al."Investigation on the interaction between a heterocyclic aminal derivative, sbdc, and human serum albumin".Colloids and surfaces b-biointerfaces 61.1(2008):75-80.

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来源:中国科学院大学

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