摘要
目的:探究表没食子儿茶素(EGC)与人血清白蛋白(HSA)的相互作用机制,明确其结合模式、类型及对HSA构象的影响。方法:采用荧光光谱法、圆二色谱(CD)和分子对接技术研究EGC与HSA的相互作用。结果:EGC对HSA的荧光淬灭为静态淬灭,属于中等结合,且结合位点比为1∶1。热力学分析显示结合过程由疏水作用驱动且自发进行。CD结果表明EGC结合导致HSA的α-螺旋和无规则卷曲含量下降,β-折叠和β-转角含量增加。分子对接证实EGC结合于HSA的Sudlow位点Ⅰ,并且氢键不可忽略。结论:EGC通过疏水作用和氢键与HSA的Sudlow位点Ⅰ特异性结合,引起HSA构象变化,该结果为探讨EGC在体内的运输、代谢等提供了理论依据。
Objective:This study aimed to explore the interaction mechanism between epigallocatechin(EGC)and human serum albumin(HSA),clarify its binding mode,type,and the impact on the conformation of HSA.Methods:Fluorescence spectroscopy,circular dichroism(CD),and molecular docking were used to investigate the interaction between EGC and HSA.Results:The fluorescence quenching of HSA by EGC was static quenching,indicating a moderate binding with a binding site ratio of 1∶1.Thermodynamic analysis showed that the binding process was driven by hydrophobic interactions and was spontaneous.CD results indicated that the binding of EGC led to a decrease in the content of α-helix and random coil in HSA,and an increase in the content of β-sheet andβ-turn.Molecular docking confirmed that EGC bound to Sudlow site I of HSA,and hydrogen bonds were not negligible.Conclusion:EGC specifically binds to Sudlow site I of HSA through hydrophobic interactions and hydrogen bonds,causing conformational changes in HSA,which provides a theoretical basis for exploring the transport and metabolism of EGC in vivo.
作者
吕韶利
邹丽平
谢家扬
欧阳熹原
袁诗语
王旺
LYU Shaoli;ZOU Liping;XIE Jiayang;OUYANG Xiyuan;YUAN Shiyu;WANG Wang(Key Laboratory of Infection and Immunity,Health Commission of Jiangxi Province,Nanchang Medical College,Nanchang 330052,China)
出处
《山东化工》
2026年第1期27-31,共5页
Shandong Chemical Industry
基金
南昌医学院自然科学基金(NYXJ-2024-035)
南昌医学院博士科研启动基金(NYB22001)
南昌医学院病原生物与免疫科研创新团队(NYTD202408)。
