a School of Chemistry and Chemical Engineering , Liaocheng University , Liaocheng , China.
b Institute of BioPharmaceutical Research , Liaocheng University , Liaocheng , China.
J Biomol Struct Dyn. 2019 Jul;37(11):2776-2788. doi: 10.1080/07391102.2018.1505550. Epub 2018 Nov 13.
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.
绿茶作为一种癌症预防剂引起了极大的关注。茶多酚与血清白蛋白的相互作用可能会影响药物的疗效。在 pH 值为 7.4 和不同温度下，单独或与人血清白蛋白 (HSA) 结合的 (-)-表没食子儿茶素-3-没食子酸酯 (EGCG)、(-)-表儿茶素-3-没食子酸酯 (ECG) 和替加氟 (TF) 的相互作用通过光谱法、等温滴定微量热法 (ITC) 和分子对接进行了研究。与 HSA 的结合亲和力顺序为 EGCG > ECG > TF，相互作用是自发的和放热的。三元体系研究表明，一种成分的存在会阻碍另一种成分与 HSA 的结合。配体存在时 HSA 的二级结构略有改变。位点标记实验和分子对接表明，EGCG 和 ECG 主要与亚域 IIA 和 ΙΙΙA 结合，而 TF 与亚域 ΙΙA 和 ΙB 结合。结果表明，ECG 和 EGCG 的存在会影响 TF 与 HSA 的结合，并增加 TF 的游离浓度。获得的结果将为茶成分和药物同时给药时可能发生的干扰提供有益信息。Ramaswamy H. Sarma 交流。
