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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 被引量:10

Intermolecular Hydrogen Bond between Protein and Flavonoid and Its Cont ribution to the Stability of the Flavonoids
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摘要 运用三维荧光光谱、紫外可见分光光谱以及傅里叶红外光谱等手段研究了蛋白与黄酮分子的相互作用,并结合相关性分析的统计学手段分析了蛋白与黄酮分子相互作用方式对黄酮稳定性的影响。实验结果表明,疏水相互作用是三种蛋白与黄酮分子之间主要的作用力,在牛血清白蛋白与黄酮的结合中有氢键的参与,同时发现在牛血清白蛋白体系中黄酮的稳定性明显增强。通过相关性分析证明蛋白对黄酮稳定性的提高与两者之间的分子间氢键有关,氢键结合作用越强蛋白对黄酮保护越明显。 The interactions between three proteins(BSA,ly sozyme and myoglobin) and three flavonoids(quercetin,kaempferol and rutin) wer e analyzed,using three-dimensional fluorescence spectrometry in combination wi th UV-Vis spectrometry and Fourier transform infrared(FTIR) spectroscopy.The st abilities of unbound flavonoids and protein-bound flavonoids were compared.The correlation between the interaction and stability was analyzed.The results show ed that the hydrophobic interaction was the main binding code in all proteins an d flavonoids systems.However,the hydrogen bond has been involved merely in the BSA system.The stability of all three flavonoids(quercetin,kaempferol and ru tin) was improved by BSA.There was a great correlation between the hydrogen bon ding and the stability of the flavonoids in the presence of BSA.It suggested th at the protection of BSA on the flavonoids was due to the intermolecular hydroge n bonding between BSA and flavonoid,and the stronger hydrogen bonding resulted in more protection.
出处 《光谱学与光谱分析》 SCIE EI CAS CSCD 北大核心 2012年第1期108-112,共5页 Spectroscopy and Spectral Analysis
基金 国家“十二五”科技支撑计划项目(2011BAD23B04,2011BAD09B00)资助
关键词 蛋白 黄酮 稳定性 氢键 三维荧光光谱 紫外可见光谱 傅里叶变换红外光谱 Protein Flavonoids Stability Hydrogen bond Fluorescence spectrometry UV spectrometry FT infraed spectrometry
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参考文献15

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