摘要
采用紫外光谱、荧光光谱和圆二色光谱方法联合分子对接和分子动力学模拟技术研究了3-吲哚丁酸(IBA)与人血清白蛋白(HSA)的相互作用,探究了两者相互作用对HSA结构的影响。结果表明,IBA能够与HSA结合形成复合物,增加反应体系的荧光强度,氢键和范德华力为IBA与HSA结合的主要驱动力,其结合常数在103数量级。位点竞争实验和分子对接表明,IBA结合在HSA亚域ⅡA的SiteⅠ位点,并通过范德华力与氨基酸残基Ser192、Tyr150、Glu196、Ala291、His288和Glu292发生相互作用,且与Arg257和Glu153形成氢键。IBA的结合使得HSA的多肽链收缩,巯基含量减少,α-螺旋含量增加和β-折叠含量降低。分子动力学模拟进一步表明,IBA与HSA结合使得HSA的表面疏水性下降,极性增加,分子结构刚性程度减弱。这些发现为从分子水平上认识IBA与HSA的作用机制及IBA的潜在毒性提供理论基础。
The interaction between 3-indolebutyric acid(IBA)and human serum albumin(HSA)was investigated by multispectral methods combined with molecular docking and molecular dynamics techniques,and the effect on HSA structure was also explored.The results showed that IBA could form a complex with HSA to cause an increase in the fluorescence intensity of the reaction system,hydrogen bonds and van der Waals force were the main driving forces for the binding of IBA with HSA,and the binding constant was 103 order of magnitude.The site competition experiments and molecular docking indicated that IBA mainly bound to the Site Ⅰ of subdomain ⅡA in HSA,and interacted with the amino acid residues Ser192,Tyr150,Glu196,Ala291,His288 and Glu292 through van der Waals force,and formed hydrogen bonds with Arg257 and Glu153.IBA binding to HSA resulted in the contraction of polypeptide chain of HSA with decrease of sulfhydryl group content,and increase of α-helix content and decrease of β-sheet content.Molecular dynamics simulation further clarified that the binding of IBA and HSA led to decrease of surface hydrophobicity of HSA and increase of polarity,and weakening the rigidity of molecular structure.These findings may provide the theoretical basis for understanding the interacton mechanism of IBA with HSA and the potential toxicity of IBA at the molecular level.
作者
张国文
张丹
吴健妹
ZHANG Guowen;ZHANG Dan;WU Jianmei(State Key Laboratory of Food Science and Technology,Nanchang University,Nanchang 330047,China)
出处
《南昌大学学报（工科版）》
CAS
2023年第1期1-8,共8页
Journal of Nanchang University(Engineering & Technology)
基金
国家自然科学基金面上项目(22078143)
江西省自然科学基金重点项目(20212ACB205010)
食品科学与技术国家重点实验室课题(SKLF-ZZB-202136、SKLF-ZZA-201912)。
关键词
3-吲哚丁酸
人血清白蛋白
相互作用
分子模拟
3-indolebutyric acid
human serum albumin
interaction
molecular simulation
