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作 者:赵新宇 陈林[1] 杨瑞[1] 赵振龙 张宇[1] 贾丽华[1] ZHAO Xin-yu;CHEN Lin;YANG Rui;ZHAO Zhen-long;ZHANG Yu;JIA Li-hua(School of Chemistry and Chemical Engineering,Qiqihar University,Heilongjiang Qiqihar 161006,China)
机构地区:[1]齐齐哈尔大学化学与化学工程学院,黑龙江齐齐哈尔161006
出 处:《齐齐哈尔大学学报(自然科学版)》2024年第3期53-58,共6页Journal of Qiqihar University(Natural Science Edition)
基 金:黑龙江省省属高校基本科研业务费项目(145109102)。
摘 要:为了获得水溶性芘衍生物与血清白蛋白的结合特性,研究了两亲芘衍生物(C_(12)PDA)与牛血清白蛋白(BSA)在中性缓冲溶液中的相互作用。首先,通过吸收和荧光光谱研究了C_(12)PDA与BSA的相互作用。结果表明,C_(12)PDA对BSA的荧光猝灭属于静态猝灭,疏水作用是两者之间的主要作用力。进一步利用同步荧光、三维荧光、圆二色光谱及分子对接模拟计算方法,研究了C_(12)PDA对BSA构象的影响以及结合方式。结果表明,C_(12)PDA与BSA的多个氨酸残基存在分子间氢键等相互作用,C_(12)PDA使BSA的α-螺旋结构含量减少。In order to obtain the binding properties of water-soluble pyrene derivatives with serum albumin,the interaction between a pyrene derivative(C_(12)PDA)and bovine serum albumin(BSA)in neutral buffer solution was studied.Firstly,the interaction between C_(12)PDA and BSA was studied by absorption and fluorescence spectra.The results show that the fluorescence of BSA is quenched by C_(12)PDA due to static quenching,and the hydrophobic effect is the dominant force in the complex forming.The effect of C_(12)PDA on the conformation of BSA and its binding mode were studied by synchronous fluorescence,three-dimensional fluorescence,circular dichroism and molecular docking simulation.The results showed that there were intermolecular hydrogen bond interactions between C_(12)PDA and several amino acid residues of BSA.Moreover,the content ofα-helical structure of BSA was reduced by C_(12)PDA.
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