Drug-binding Specificity of Human Serum Albumin Investigated by Molecular Modeling Approach
To develop and validate a rapid method for determining the binding site of human serum albumin (HSA) with pharmaceutical candidates, docking of six known site markers to HSA have been calculated by using the Affinity module of Insight II 2005 software. The results are well-consistent with the literatures report. Further the molecular dynamic (MD) method has been applied to calculate the binding of two carbohybrids (SNDC and SBDC) with HSA and the outcomes are in accord with the data obtained by the traditional fluorescence techniques. Both methods suggested that the primary binding site of OTA, SNDC and SBDC is located in subdomain ⅡA of HSA. The distance, r, between donor and acceptor was obtained according to the Forsters theory of non-radiation energy transfer are 3.12 nm and 2.79 nm for SNDC-HSA and SBDC-HSA complexes, respectively, and hence confirm that the MD method can be applied to investigate complexation of drugs to HAS.
human serum albumin molecular docking site markers
Qiuju Zhou Junfeng Xiang Yalin Tang Zhanli Wang Guangzhi Xu
Beijing National Laboratory for Molecular Sciences (BNLMS), Center for Molecular Sciences, State Key Beijing National Laboratory for Molecular Sciences (BNLMS), Center for Molecular Sciences, State Key NeoTrident Technology Limited, Beijing Office, Beijing, 100080, P. R. China
国际会议
杭州
英文
976-982
2007-04-01（万方平台首次上网日期，不代表论文的发表时间）