还原型辅酶烟酰胺腺嘌呤二核苷酸与人血清白蛋白相互作用的研究  

Study on the Interaction of Reduced Nicotinamide Adenine Dinucleotide with Human Serum Albumin

作　　者：霍彩霞[1] 何丽君[1] 常国华[1] 赵国虎[1] 兰银伟[1] 

机构地区：[1]兰州城市学院化学与环境科学学院,甘肃兰州730070

出　　处：《分析科学学报》2013年第4期531-534,共4页Journal of Analytical Science

基　　金：甘肃省教育厅硕士生导师项目(0811-07);甘肃省科技厅自然科学基金(No.096RJZA064)

摘　　要：运用荧光光谱、紫外光谱和计算机模拟分子对接等技术,研究了在模拟生理条件下还原型辅酶烟酰胺腺嘌呤二核苷酸(NADH)与人血清白蛋白(HSA)的作用方式及热力学特征。结果表明,NADH与人血清白蛋白的荧光猝灭机理属于静态猝灭;NADH与HSA在温度283K和310K时的结合常数和结合位点数分别为1.972×104 L.mol-1、0.9657和1.468×104 L.mol-1、0.9105,通过热力学计算得到反应的热力学参数;同步荧光光谱表明NADH使色氨酸残基的微环境亲水性增强;分子模型研究表明,二者通过疏水力、静电力和氢键共同作用结合。The interaction mechanism and thermodynamic characteristic between reduced nicotinamide adenine dinucleotide（NADH） and human serum albumin（HSA） have been investigated by fluorescence spectrometry,UV spectroscopy and molecular modeling. The fluorescence quenching of HSA by NADH indicates that the mechanism is a static quenching. The bonding constants and the binding point numbers of NADH and HSA are K,1 =1. 972X104L·mol ^-1 ,nl =0. 9657（283 K） and KA2 =1. 468X 104L·mol ^-1 , n2 = 0.9105 （310 K）, respectively. The thermodynamic parameters were calculated according to the Van＇t Hoff equation. Synchronous spectra shows that the microenvironment of tryptophan residues is more hydrophilic when NADH is added. Molecular modeling suggests that NADH is located in subdomain II A into HSA by hydrophobic forces,electrostatic and hydrogen bond.

关 键 词：烟酰胺腺嘌呤二核苷酸 人血清白蛋白 荧光光谱法 紫外光谱法 分子对接 

分 类 号：O657.3[理学—分析化学]