基于光谱分析的鞣花酸和尿石素A~D与HSA相互作用机理研究  

Study on the Interaction Mechanism of Ellagic Acid and Urolisine A~D With HSA Based on Spectral Analysis

作　　者：谢星 程鑫鹏 张露[1] 罗晶 王乐怀 林文静 卢菲艳 涂宗财[1,2] XIE Xing;CHENG Xin-peng;ZHANG Lu;LUO Jing;WANG Le-huai;LIN Wen-jing;LU Fei-yan;TU Zong-cai(Department of Food Nutrition and Health,College of Health,Jiangxi Normal University,Nanchang 330022,China;State Key Laboratory of Food Science and Resources,Nanchang University,Nanchang 330047,China)

机构地区：[1]江西师范大学健康学院食品营养与健康系,江西南昌330022 [2]南昌大学食品科学与资源挖掘全国重点实验室,江西南昌330047

出　　处：《光谱学与光谱分析》2025年第1期282-290,共9页Spectroscopy and Spectral Analysis

基　　金：国家自然科学基金地区项目(31860475);江西省青年科学基金项目(20224BAB215051);江西省教育厅项目(GJJ2200382)资助。

摘　　要：采用光谱分析结合分子模拟技术探究了鞣花酸(EA)及其代谢产物尿石素A~D(UA~D)与人血清白蛋白(HSA)的相互作用机理,有助于解析其药理毒性和药效。研究结果表明EA和UA~D能与HSA以1∶1的摩尔比例结合并通过静态方式猝灭HSA的荧光。UA和UC与HSA结合是氢键和范德华力驱动的放热过程,而EA和UD与HSA结合疏水相互作用驱动的吸热过程。三维荧光图谱分析表明UC~D和EA与UA~B分别增加了HSA色氨酸和酪氨酸微环境的亲水性和疏水性。分子模拟分析结果表明,EA和UA~D与HSA的活性氨基酸残基Lys436、Asp187、Lys432、Arg485、Leu430、Leu4、Ile388、Tyr411等形成氢键,与氨基酸残基Ala191、Val456、Lys199和Trp214之间存在疏水相互作用,证明其主要通过氢键和范德华力与HSA结合,屏蔽HSA的糖基化位点,抑制其糖基化。可为EA和UA~D作为糖基化抑制剂用于治疗糖尿病并发症奠定理论基础。Spectroscopy and molecular simulation technologies investigated The interaction mechanism between ellagic acid(EA)and urolithin A~D(UA~D)with HSA,which helped explore its pharmacotoxicity and efficacy.The results indicated that EA and UA~D could bind with HSA at a molar ratio of 1∶1 and quench its fluorescence via a static mechanism.The binding of UA and UC with HSA was exothermic and driven by hydrogen bonding and van der Waals force.The binding of EA and UD with HSA was endothermic and driven by hydrophobic interaction.The three-dimensional fluorescence spectrum analysis exhibited that the addition of EA and UC,UD,UA,and UB enhanced the hydrophilicity and hydrophobicity of tyrosine and tryptophan microenvironments of HSA,respectively.The molecular simulation analysis showed that EA and UA~D formed hydrogen bonds with active amino acid residues Lys436,Asp187,Lys432,Arg485,Leu430,Leu4,Ile388 and Tyr411,and formed hydrophobic interaction with active amino acid residues Ala191,Val456,Lys199 and Trp214,which proved that they were majorly bound to HSA by hydrogen bonds and van der Waalsforce,and then screened glycation sites and inhibited HSA glycation.This study could provide a theoretical basis for developing EA and UA~D as non-enzyme glycation inhibitors to treat diabetic complications.

关 键 词：人血清白蛋白 糖基化 相互作用机理 光谱分析 鞣花单宁及其代谢产物 

分 类 号：TS201.2[轻工技术与工程—食品科学]