现代食品科技2024，Vol.40Issue(4)：84-94,11.DOI:10.13982/j.mfst.1673-9078.2024.4.0426
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
摘要
Abstract
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(0.35～1.78 μmol/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 2.0 Å and 2.7 Å hydrogen bonds with the Lys504 and Thr190 residues in BSA,respectively,whereas(3R,3'R)-AST formed a 2.9 Å hydrogen 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Key words
astaxanthin/optical isomer/bovine serum albumin/interaction引用本文复制引用
郑钦生,周乐松,张俊林,邹晓君,曹庸,刘晓娟..虾青素立体异构体与牛血清白蛋白的相互作用[J].现代食品科技,2024,40(4):84-94,11.基金项目
国家自然科学基金项目(32172195) （32172195）
广东省自然科学基金项目(2021A1515012158) （2021A1515012158）
