基于光谱法及分子对接技术的猪血红蛋白与儿茶素相互作用研究  

Preliminary Study on the Interaction between Porcine Hemoglobin and Catechin Based on Spectroscopy and Macromolecular Docking Technique

作　　者：刘丽莉[1,2,3,4] 陈卉 郭净芳 张潇丹 苏克楠 于影 LIU Lili;CHEN Hui;GUO Jingfang;ZHANG Xiaodan;SU Kenan;YU Ying(College of Food&Bioengineering,Henan University of Science and Technology,Luoyang,Henan 471023;National Experimental Teaching Demonstration Center for Food Processing and Safety,Luoyang,Henan 471023;Henan International Joint Laboratory of Food Processing and Quality and Safety Control,Luoyang,Henan 471023;Henan Engineering Technology Research Center of Food Microbiology,Luoyang,Henan 471023)

机构地区：[1]河南科技大学食品与生物工程学院,河南洛阳471023 [2]食品加工与安全国家级实验教学示范中心,河南洛阳471023 [3]河南省食品加工与质量安全控制河南省国际联合实验室,河南洛阳471023 [4]食品微生物河南省工程技术研究中心,河南洛阳471023

出　　处：《核农学报》2024年第6期1117-1124,共8页Journal of Nuclear Agricultural Sciences

基　　金：河南省重大科技专项(221100110500);洛阳市社会发展专项(2101021A);国家重点研发计划科技型中小企业项目(2022YFF1101600);中部地区科技创新领先人才计划(234200510020)。

摘　　要：为增强猪血红蛋白(PHb)结构的稳定性,提高其应用价值,将天然抗氧化剂儿茶素(C)与PHb进行互作,以期稳定PHb的结构。采用紫外可见光谱、荧光光谱、傅里叶红外光谱和扫描电镜研究C与PHb的相互作用,并通过分子模拟对接技术表征儿茶素-猪血红蛋白复合物(C-PHb)的形貌和结构。结果表明,添加C前后,PHb的紫外吸收光谱发生明显变化;荧光光谱结果表明,C能有效猝灭PHb内源荧光且为自由发生的静态猝灭,猝灭常数(Kq)为7.5×10^(10)L·mol^(-1)·s^(-1),作用力主要为范德华力、氢键和疏水作用力。同时,相较于PHb,C-PHb的蛋白质二级结构发生改变,表现为β-折叠含量增高,α-螺旋、β-转角和无规卷曲含量降低。此外,分子对接模型进一步验证了C可与PHb进行相互作用。综上,C可与PHb互作以稳定其结构。本研究可为制备具有抗氧化性质的PHb复合物提供理论支持和可行性依据。In order to improve the shortcomings of unstable properties of porcine hemoglobin(PHb)and its application value,the natural antioxidant catechins(C)and PHb were interacted with PHb to stabilize the structure of PHb.The ultraviolet-visible spectroscopy,fluorescence spectroscopy,fourier transform infrared spectroscopy and scanning electron microscopy were used to study the interaction between C and PHb,and the morphology and structure of C-PHb were characterized by molecular simulation docking technology.The ultraviolet absorption spectrum of PHb changed significantly after addition of C.The fluorescence spectroscopy results showed that C could effectively quench the endogenous fluorescence of PHb,which was a free-occurring static quenching with a quenching constant(Kq)of 7.5×10^(10) L·mol^(-1)·s^(-1).The main forces were van der Waals forces,hydrogen bonding and hydrophobic forces.Meanwhile,compared with PHb,the protein secondary structure of C-PHb changed,which was manifested by the increase ofβ-folding,and a decrease in the content ofα-helix,β-turn and random coil.In addition,the molecular docking model further verified that C can interact with PHb.Studies have shown that C can interact with PHb.This study could provide the theoretical support and feasibility basis for the preparation of PHb complexes with antioxidant properties.

关 键 词：猪血红蛋白 儿茶素 相互作用 光谱法 分子对接 

分 类 号：TS251.93[轻工技术与工程—农产品加工及贮藏工程] O657.3[轻工技术与工程—食品科学与工程]