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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

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【作者】 霍彩霞何丽君李康兰陈明凯包慧芳

【Author】 HUO Cai-xia,HE Li-jun,LI Kang-lan,CHEN Ming-kai,BAO Hui-fang(School of Chemistry and Environment Science,Lanzhou City University,Lanzhou 730070,China)

【机构】 兰州城市学院化学与环境科学学院

【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.

【Abstract】 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.

  • 【文献出处】 甘肃联合大学学报(自然科学版) ,Journal of Gansu Lianhe University(Natural Science Edition) , 编辑部邮箱 ,2013年04期
  • 【分类号】R96;O657.3
  • 【被引频次】2
  • 【下载频次】77
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