小锌配合物与球状蛋白和游离色氨酸的相互作用

J. Butkus, Shelby O’Riley, B. Chohan, Swarna Basu
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引用次数: 11

摘要

合成了8种水溶性阴离子、阳离子和中性锌配合物,并对其进行了表征。利用稳态荧光光谱技术研究了这些复合物与牛血清白蛋白(BSA)、人血清白蛋白(HSA)、溶菌酶和游离色氨酸(Trp)的相互作用。基于Stern-Volmer动力学进行了静态和动态荧光猝灭分析,Trp残基荧光强度的下降主要归因于Zn配合物与蛋白质结合并形成非荧光配合物时发生的静态猝灭。研究了配体、金属和配合物的性质在猝灭色氨酸荧光中的作用。结合常数()范围为104 ~ 1010 M−1,表明具有平面芳族特征的配合物对球状蛋白和游离色氨酸的亲和力最强。具有非芳香特征的配合物不能在Trp残基处或附近与这些蛋白质相互作用。在一定温度范围内对这些相互作用进行了研究,发现结合随着温度的升高而减弱,并且随着熵的负变化而放热。热力学参数表明,锌配合物与蛋白质的结合是一个高度自发的有利过程。
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Interaction of Small Zinc Complexes with Globular Proteins and Free Tryptophan
A series of eight water soluble anionic, cationic, and neutral zinc(II) complexes were synthesized and characterized. The interaction of these complexes with bovine serum albumin (BSA), human serum albumin (HSA), lysozyme, and free tryptophan (Trp) was investigated using steady-state fluorescence spectroscopy. Static and dynamic fluorescence quenching analysis based on Stern-Volmer kinetics was conducted, and the decrease in fluorescence intensity of the Trp residue(s) can be ascribed predominantly to static quenching that occurs when the Zn complex binds to the protein and forms a nonfluorescent complex. The role played by the nature of the ligand, the metal, and complex charge in quenching Trp fluorescence was investigated. The binding association constants () ranged from 104 to 1010 M−1 and indicate that complexes with planar aromatic features have the strongest affinity for globular proteins and free Trp. Complexes with nonaromatic features failed to interact with these proteins at or in the vicinity of the Trp residues. These interactions were studied over a range of temperatures, and binding was found to weaken with the increase in temperature and was exothermic with a negative change in entropy. The thermodynamic parameters suggest that binding of Zn complexes to the proteins is a highly spontaneous and favorable process.
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