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.
作者
刘丽莉
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)
出处
《核农学报》
CAS
CSCD
北大核心
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)。
关键词
猪血红蛋白
儿茶素
相互作用
光谱法
分子对接
porcine hemoglobin
catechin
interaction
spectroscopy
molecular docking 1124
