Effect of (–)-epicatechin-3-gallate and (–)-epigallocatechin-3-gallate on the binding of tegafur to human serum albumin as determined by spectroscopy, isothermal titration calorimetry, and molecular docking

等温滴定量热法 化学 没食子酸 量热法 对接(动物) 没食子酸丙酯 特加福 血清白蛋白 没食子酸表没食子酸酯 色谱法 多酚 生物化学 核化学 热力学 内科学 癌症 抗氧化剂 医学 护理部 物理
作者
Lixia Yuan,Min Liu,Yabo Shi,Hui Yan,Jun Han,Liying Liu
出处
期刊:Journal of Biomolecular Structure & Dynamics [Taylor & Francis]
卷期号:37 (11): 2776-2788 被引量:18
标识
DOI:10.1080/07391102.2018.1505550
摘要

Green tea has attracted great interest as a cancer prevention agent. Interactions of tea polyphenols with serum albumin may influence the efficacy of drugs. The interactions of (–)-epigallocatechin-3-gallate (EGCG), (–)-epicatechin-3-gallate (ECG), and tegafur (TF) alone or in combination with human serum albumin (HSA) at pH 7.4 and different temperatures were investigated by spectroscopic methods, isothermal titration calorimetry (ITC), and molecular docking. The binding affinities to HSA were ranked in the order of EGCG > ECG > TF, and the interactions were spontaneous and exothermic. Ternary system studies showed that the presence of one component hindered the binding of another component to HSA. The secondary structures of HSA were slightly altered in the presence of the ligands. Site marking experiments and molecular docking showed that EGCG and ECG mainly bound to subdomain IIA and ΙΙΙA while TF bound to subdomain ΙΙA and ΙB. Results indicated that the existence of ECG and EGCG would influence the binding of TF to HSA and can increase the free concentration of TF. Obtained results would provide beneficial information about possible interference upon simultaneous co-administration of the tea components and drugs.Communicated by Ramaswamy H. Sarma
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