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在3种酸度条件下,采用多种光谱技术对一种白杨素衍生物和牛血清白蛋白的相互作用进行了研究。结果表明该衍生物和牛血清白蛋白可形成基态复合物,静态、动态猝灭方式同时存在,以静态猝灭为主。通过计算获得了在不同温度及酸度条件下的结合常数及结合位点数。该衍生物在碱性条件下和牛血清白蛋白的结合能力较强。在pH 7.40的生理条件下,该衍生物具有比白杨素更强的结合能力。根据该衍生物和牛血清白蛋白结合的热力学参数,确定了二者之间主要为疏水作用力。根据Foerster非辐射能量转移理论确定了二者的作用距离。同步荧光光谱显示该衍生物可与蛋白中色氨酸和酪氨酸残基发生相互作用,但对其周围的局部构象没有明显的影响。红外光谱显示该衍生物可以改变蛋白的二级结构。
The interaction of a chrysin derivative with bovine serum albumin was studied using a variety of spectroscopic techniques under three acidity conditions. The results show that the derivative and bovine serum albumin can form the ground state complex, static and dynamic quenching modes coexist, mainly static quenching. The binding constants and number of binding sites under different temperature and acidity conditions were calculated. This derivative has strong binding ability to bovine serum albumin under alkaline conditions. Under physiological conditions at pH 7.40, this derivative has stronger binding capacity than chrysin. According to the thermodynamic parameters of the derivative binding to bovine serum albumin, it was confirmed that the hydrophobic interaction between the two was mainly. According to Foerster non-radiative energy transfer theory to determine the distance between the two. Synchronous fluorescence spectroscopy showed that this derivative interacted with tryptophan and tyrosine residues in proteins, but had no obvious effect on its local conformation. Infrared spectroscopy shows that the derivative can change the secondary structure of the protein.