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OA北大核心CSTPCD

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 7.5×1010 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 of β-folding,and a decrease in the content of α-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.