Interaction of lafutidine in binding to human serum albumin in gastric ulcer therapy: STD-NMR, WaterLOGSY-NMR, NMR relaxation times, Tr-NOESY, molecule docking, and spectroscopic studies
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- 作者：Hongqin Yang ; Yanmei Huang ; Jiawei He ; Shanshan Li ; Bin Tang ; Hui Li ; lihuilab@sina.com" class="auth_mail" title="E-mail the corresponding author
- 关键词：Human serum albumin ; Lafutidine ; STD and WaterLOGSY-NMR ; Relaxation experiments and tr-NOESY ; Molecule docking ; Conformational changes
- 刊名：Archives of Biochemistry and Biophysics
- 出版年：2016
- 出版时间：15 September 2016
- 年：2016
- 卷：606
- 期：Complete
- 页码：81-89
- 全文大小：1626 K
文摘
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STD and WaterLOGSY-NMR were used to determine the binding between LAF and HSA.
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Competitive NMR experiments indicated that LAF preferentially bound to site II of HSA.
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Relaxation experiment indicated that pyridyl group was spatially close to the aromatic residues of HSA.
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The bioactive conformation of LAF was identified by tr-NOESY experiment.
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žConformation changes of HSA induced by its interaction with LAF.