所属单位：化学与化工学院

发表刊物：Bull. Korean Chem. Soc.

关键字：中文关键字：牛血清白蛋白；相互作用；光谱法，英文关键字：Bovine serum albumin (BSA); Interaction; Spectrome

摘要：We studied the interaction of 3,3′,3′′,3′′′–ethylenetetrakis–4–hydroxycoumarin (EHC) with bovine serum albumin (BSA) in acetate buffer and phosphate buffer with different pH values by UV–vis absorption spectrometry and fluorescence spectrometry respectively. It was found that the pH values of the buffer solutions had an effect on the interaction process. In acetate buffer of pH 4.70, the carbonyl groups in EHC bound to the amino groups in BSA by means of hydrogen bond and van der Waals force, which made the extent of peptide chain in BSA changed. By contrast, in phosphate buffer of pH 7.40, hydrophobic force played a major role in the interaction between EHC and BSA, while the hydrogen bond and van der Waals force were also involved in the interaction. The results of spectrometry indicated that BSA could enhance the fluorescence intensity of EHC by forming a 1:1 EHC–BSA fluorescent complex through static mechanism at pH 4.70 and 7.40 respectively. Furthermore, EHC bound on site Ⅰ in BSA.

备注：董社英

第一作者：董社英

论文类型：期刊论文

卷号：卷：32

期号：期：

页面范围：页：2949-2954

是否译文：否

发表时间：2011-06-01