化学
圆二色性
氢键
对接(动物)
疏水效应
乳清蛋白
结合常数
荧光光谱法
荧光
蛋白质二级结构
结晶学
立体化学
结合位点
色谱法
生物化学
有机化学
分子
量子力学
医学
物理
护理部
作者
Jing Cheng,Jianhua Liu,Govindarajan Prasanna,Pu Jing
标识
DOI:10.1016/j.ijbiomac.2017.07.119
摘要
The interaction of β-Lactoglobulin (β-Lg) with cyanidin-3-O-glucoside (C3G) was characterized using fluorescence, circular dichroism spectroscopy, and docking studies under physiological conditions. Fluorescence studies showed that β-Lg has a strong binding affinity for C3G via hydrophobic interaction with the binding constant, Ka, of 3.14 × 104 M−1 at 298 K. The secondary structure of β-Lg displayed an increase in the major structure of β-sheet upon binding with C3G, whereas a decrease in the minor structure of α-helix was also observed. In addition, evidenced by near UV-CD, the interaction also disrupted the environments of Trp residues. The molecular docking results illustrated that both hydrogen bonding and the hydrophobic interaction are involved as an acting force during the binding process. These results may contribute to a better understanding over the enhanced physicochemical proprieties of anthocyanins due to the complexation with milk proteins.
科研通智能强力驱动
Strongly Powered by AbleSci AI