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| Studies on Interaction between Pentafluoropropioic Acid and Human Serum Albumin by Spectroscopy and Computional Simulations |
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| DOI： |
| KeyWord:pentafluoropropionic acid(IPC-PFFA-3 ) human serum albumin(HSA) molecular docking molecular dynamics(MD) simulation fluorescence spectroscopy |
| Author | Institution |
| YI Zhong-sheng*,WANG Hai-yang,WU Zhi-wei,ZHANG Ai-qian |
1.桂林理工大学化学与生物工程学院;2.中国科学院生态环境研究中心环境化学与生态毒理学国家重点实验室 |
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| Abstract: |
| The interaction of pentafluoropropionic acid(IPC-PFFA-3) with human serum albumin(HSA) was studied using molecular docking,molecular dynamics(MD) simulation,fluorescence spectroscopy,synchronous fluorescence and competition experiments.The results of the molecular docking indicated that the binding force between IPC-PFFA-3 and HSA was hydrogen bond.Fluorescence data revealed that the fluorescence quenching of HSA by IPC-PFFA-3 was a static quenching procedure.The thermodynamic parameters showed that binding was spontaneous and was driven mainly by hydrogen bond.Competitive drug displacement results suggested that the binding site of IPC-PFFA-3 with HSA lie on Sudlows site Ⅱ.The experimental results were supported by the molecular docking.MD and synchronous fluorescence suggested that HSA does have a sight conformational change when it binds with IPC-PFFA－3 and the structure of HSA-IPC-PFFA-3 is very stable. |
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