光谱-分子模拟法分析杨梅素与人血清白蛋白的分子作用机制  

Analysis on molecular interaction mechanism of myricetin binding with human serum albumin by spectroscopy and molecular modeling method

作　　者：张大维 宋宁 刘语 刘铮铮 史博文 ZHANG Dawei;SONG Ning;LIU Yu;LIU Zhengzheng;SHI Bowen(Department of Psychiatry,the First Affiliated Hospital of Xi'an Jiaotong University,Xi'an 710061;School of Pharmacy,Xi'an Jiaotong University,Xi'an 710061;Anesthesia Operation Center,Xi'an International Medical Center,Xi'an 710075)

机构地区：[1]西安交通大学第一附属医院精神卫生科,西安710061 [2]西安交通大学医学部药学院,西安710061 [3]西安国际医学中心麻醉手术中心,西安710075

出　　处：《分析试验室》2021年第3期351-356,共6页Chinese Journal of Analysis Laboratory

摘　　要：在模拟生理条件下,用多种光谱法结合分子对接法测定了杨梅素(MY)与人血清白蛋白(HSA)的相互作用。研究结果表明,MY能够明显猝灭HSA的荧光,MY与HSA的相互作用为复合式静态结合过程,结合强度较强。热力学和分子对接结果表明,MY与HSA是自发结合的,维持MY与HSA的相互作用力主要是氢键和范德华力。能量转移结果表明,MY与HSA的结合距离小于7 nm,说明MY与HSA间可以发生能量转移。MY对HSA的结构域微区构象产生了影响,使结合位域的疏水性发生了改变。本研究阐述了MY与HSA的相互作用分子机制,为天然小分子在体内转运等提供了有用信息。Under simulated physiological conditions,the interaction between myricetin(MY) and human serum albumin(HSA) was determined by various spectroscopic methods combined with molecular docking.The results showed that MY could obviously quench the fluorescence of HSA,and the interaction between MY and HSA was a combined static binding process with strong binding strength.The results of thermodynamics and molecular docking demonstrated that the interaction between MY and HAS was spontaneous.The main forces to drive the interaction between MY and HSA were hydrogen bond and Van der Waals force.The results of energy transfer illustrated that the binding distance r between MY and HSA was less than 7 nm,which indicated that the energy transfer occurred between them.The conformation of HSA domain was affected by MY,leading to the hydrophobicity changes of the binding domain.In this study, the molecular mechanism of the interaction between MY and HSA was comprehensively described,which provides useful information for the transport of natural small molecules in vivo.

关 键 词：杨梅素 人血清白蛋白 光谱 分子模拟 

分 类 号：O657.3[理学—分析化学]