Molecular mechanism of the binding of 3,4,5-tri-O-caffeoylquinic acid to human serum albumin: Saturation transfer difference NMR, multi-spectroscopy, and docking studies.

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第一作者： Bin,Tang

第一单位： College of Chemical Engineering, Sichuan University, Chengdu 610065, PR China.

作者： Bin,Tang ^[1] ; Yanmei,Huang ^[1] ; Hongqin,Yang ^[1] ; Peixiao,Tang ^[1] ; Hui,Li ^[2]

作者单位： College of Chemical Engineering, Sichuan University, Chengdu 610065, PR China. ^[1] College of Chemical Engineering, Sichuan University, Chengdu 610065, PR China. Electronic address: lihuilab@sina.com. ^[2]

关键词 Human serum albumin Molecular docking NMR Polyphenol Saturation transfer difference Spectroscopy

主题词人类(Humans);奎尼酸(Quinic Acid);血清白蛋白(Serum Albumin);光谱分析(Spectrum Analysis);热力学(Thermodynamics)

DOI 10.1016/j.jphotobiol.2016.10.017

PMID 27768950

发布时间 2017-03-28

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Journal of photochemistry and photobiology. B, Biology

2016年165卷

24-33页

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Molecular mechanism of the binding of 3,4,5-tri-O-caffeoylquinic acid to human serum albumin: Saturation transfer difference NMR, multi-spectroscopy, and docking studies.

Journal of photochemistry and photobiology. B, Biology

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Journal of photochemistry and photobiology. B, Biology

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Molecular mechanism of the binding of 3,4,5-tri-O-caffeoylquinic acid to human serum albumin: Saturation transfer difference NMR, multi-spectroscopy, and docking studies.

Journal of photochemistry and photobiology. B, Biology

相似文献

Journal of photochemistry and photobiology. B, Biology

相关期刊

检索历史清除