氨甲苯酸与人血清白蛋白相互作用的荧光法研究  

Study on the Interaction of 4-Aminomethylbenzoic Acid with Human Serum Albumin by Fluorescence Spectroscopy

作　　者：霍彩霞[1] 何丽君[1] 李康兰[1] 陈明凯[1] 包慧芳[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：《兰州文理学院学报（自然科学版）》2013年第4期47-50,共4页Journal of Lanzhou University of Arts and Science(Natural Sciences)

摘　　要：采用荧光光谱法研究了不同温度下氨甲苯酸与人血清白蛋白(HSA)的结合反应.结果表明:氨甲苯酸对HSA的荧光猝灭机制主要为静态猝灭,与HSA之间形成了1∶1的复合物,结合常数与结合位点数n分别为3.686×103,0.9253(298K)和1.671×103 L.mol-1.s-1,0.8982(310K),其作用力以氢键和范德华力为主.同步荧光光谱表明氨甲苯酸使色氨酸残基的疏水性减弱.The interaction of 4-aminomethyl benzoic acid(AMB) and human serum albumin(HSA) under different temperature was studied by fluorescence spectrum.The results showed that 4-aminomethyl benzoic acid could induce endogenous fluorescence quenching of HSA under a mechanism of static quenching.The 1∶1 complexes were formed between AMB and HSA.The binding constants KA and the number of binding sites n were determined to be 3.686×103,0.9253(298K) and 1.671×103 L·mol-1·s-1,0.8982(310K),respectively.The driving forces were mainly hydrogen bond and Vander Waals.Synchronous spectra showed tryptophan residue was more hydrophilic when AMB was added.

关 键 词：氨甲苯酸(AMB) 人血清白蛋白 荧光光谱法 同步荧光光谱 

分 类 号：N[自然科学总论]