College of Food Science & Nutritional Engineering, China Agricultural University, Key Laboratory of Functional Dairy Science of Beijing and Ministry of Education, Beijing 100083, China
Abstract：The interactions between three proteins (BSA, lysozyme and myoglobin) and three flavonoids (quercetin, kaempferol and rutin) were analyzed, using three-dimensional fluorescence spectrometry in combination with UV-Vis spectrometry and Fourier transform infrared (FTIR) spectroscopy. The stabilities of unbound flavonoids and protein-bound flavonoids were compared. The correlation between the interaction and stability was analyzed. The results showed that the hydrophobic interaction was the main binding code in all proteins and flavonoids systems. However, the hydrogen bond has been involved merely in the BSA system. The stability of all three flavonoids (quercetin, kaempferol and rutin) was improved by BSA. There was a great correlation between the hydrogen bonding and the stability of the flavonoids in the presence of BSA. It suggested that the protection of BSA on the flavonoids was due to the intermolecular hydrogen bonding between BSA and flavonoid, and the stronger hydrogen bonding resulted in more protection.
方 茹，冷小京*，吴 夏，李 琦，郝瑞芳，任发政，景 浩* . 三种蛋白和黄酮结合物中氢键与黄酮稳定性相关性分析研究[J]. 光谱学与光谱分析, 2012, 32(01): 108-112.
FANG Ru, LENG Xiao-jing*, WU Xia, LI Qi, HAO Rui-fang, REN Fa-zheng, JING Hao* . Intermolecular Hydrogen Bond between Protein and Flavonoid and Its Contribution to the Stability of the Flavonoids. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2012, 32(01): 108-112.
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