虾青素立体异构体与牛血清白蛋白的相互作用  

Interactions of Astaxanthin Optical Isomers with Bovine Serum Albumin

作　　者：郑钦生 周乐松 张俊林 邹晓君 曹庸[1] 刘晓娟[1] ZHENG Qinsheng;ZHOU Lesong;ZHANG Junlin;ZOU Xiaojun;CAO Yong;LIU Xiaojuan(College of Food Science,South China Agricultural University,Guangdong Provincial Key Laboratory of Nutraceuticals and Functional Foods,Guangzhou 510642,China)

机构地区：[1]华南农业大学食品学院,广东省功能食品活性物重点实验室,广东广州510642

出　　处：《现代食品科技》2024年第4期84-94,共11页Modern Food Science and Technology

基　　金：国家自然科学基金项目(32172195);广东省自然科学基金项目(2021A1515012158)。

摘　　要：该论文采用多光谱、表面等离子共振和分子对接,研究虾青素(Astaxanthin,AST)立体异构体与牛血清白蛋白(Bovine Serum Albumin,BSA)的相互作用机制。研究发现,AST异构体均结合于BSA亚结构域ⅡA和ⅢA的交界处,并且对蛋白质的构象没有明显影响。AST异构体对BSA具有相似的结合亲和力(左旋AST 4.17×10^(-7)mol/L,右旋AST 3.91×10^(-7)mol/L)和结合动力学(慢结合、慢解离),然而在较高浓度下(0.35~1.78μmol/L)左旋AST的最高结合响应值均高于右旋AST。此外,左旋和右旋AST与BSA相互作用的焓变△H分别为-175.09和-149.42 kJ/mol,熵变△S分别为-502.72和-417.65 J/(mol·K),负值的△H和△S表明AST-BSA发生结合的主要相互作用力是氢键和范德华力。分子对接显示左旋AST与Lys504、Thr190残基形成键长为2.0Å、2.7Å的氢键,而右旋AST与Arg435残基形成键长为2.9Å的氢键。这项研究有助于阐明AST立体异构体与BSA的结合机制,并为AST异构体在血液循环中潜在的药代动力学提供重要的理论指导信息。The mechanisms underlying the interaction between the two optical isomers of astaxanthin(AST)and bovine serum albumin(BSA)were investigated based on multiple spectroscopic,surface plasmon resonance,and molecular docking analyses.Both AST isomers were found to bind to BSA at the junction of subdomains IIA and IIIA,in the absence of any significant effects on protein conformation.The two isomers had similar binding affinities[4.17×10^(-7) mol/L for(3S,3’S)-AST and 3.91×10^(-7) mol/L for(3R,3’R)-AST for]and kinetic binding processes(slow binding,slow dissociation)for BSA.However,at higher concentrations(0.35~1.78μmol/L),the highest binding response values obtained for(3S,3’S)-AST were higher than those for(3R,3’R)-AST.In addition,the change in enthalpy(△H)for the interactions between(3S,3’S)-AST and(3R,3’R)-AST and BSA were-175.09 and-149.42 kJ/mol,respectively,and the corresponding changes in entropy(△S)were-502.72 and-417.65 J/(mol·K).The negative values obtained for∆H and∆S indicate that hydrogen bonds and van der Waals forces were the main forces underlying the AST-BSA interactions.Molecular docking analysis revealed that(3S,3’S)-AST formed 2.0Åand 2.7Åhydrogen bonds with the Lys504 and Thr190 residues in BSA,respectively,whereas(3R,3’R)-AST formed a 2.9Åhydrogen bond with the Arg435 residue.Our findings in this study contribute to elucidating the mechanisms associated with the binding of AST optical isomers to BSA,and will provide important theoretical guidance for the potential pharmacokinetics of AST isomers in blood circulation.

关 键 词：虾青素 立体异构体 牛血清白蛋白 相互作用 

分 类 号：TS201.4[轻工技术与工程—食品科学]