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甲基橙皮苷和人血清白蛋白相互作用的光谱研究
引用本文:李金华,王素敏,朱金花. 甲基橙皮苷和人血清白蛋白相互作用的光谱研究[J]. 化学研究, 2013, 0(2): 176-179
作者姓名:李金华  王素敏  朱金花
作者单位:西安工业大学材料科学与化工学院;河南大学化学化工学院
基金项目:陕西省教育厅专项科研计划项目(2010JK609)
摘    要:利用荧光光谱法和红外光谱法研究了甲基橙皮苷(MH)与人血清白蛋白(HSA)的相互作用.结果表明,MH对HSA的荧光有较强的猝灭作用.在296、303、310K温度下,MH与HSA相互作用的结合常数分别为1.77×104,2.65×104,3.53×104 L·mol-1.热力学分析结果表明,MH与HSA之间的结合过程是吸热的并且是自发的;作用力以疏水作用为主,并伴随氢键作用.

关 键 词:甲基橙皮苷  人血清白蛋白  相互作用  荧光光谱  红外光谱

Interaction between methyl hesperidin and human serum albumin studied by spectrometric methods
LI Jin-hua,WANG Su-min,ZHU Jin-hua. Interaction between methyl hesperidin and human serum albumin studied by spectrometric methods[J]. Chemical Research, 2013, 0(2): 176-179
Authors:LI Jin-hua  WANG Su-min  ZHU Jin-hua
Affiliation:2(School of Materials and Chemical Engineering,Xi’an Technological University,Xi’an 710032,Shaanxi,China; 2.College of Chemistry and Chemical Engineering,Henan University,Kaifeng 475004,Henan,China)
Abstract:The interaction between methyl hesperidin (MH) and human serum albumin (HSA) under simulative physiological conditions was studied by spectroscopic methods including fluo- rescence quenching technology and Fourier transform infrared (FT-IR) spectrometry. Results reveal that MH can well quench the intrinsic fluorescence of HSA. The binding constants at 296, 303, and 310 K are 1.77×104 , 2.65×104 , and 3.53×104 L .mol-1 , respectively. Ther- modynamic analyses show that the binding process between MH and HSA is endothermic and spontaneous, and the interaction is dominated by hydrophobic interaction, accompanied by hy- drogen bonding.
Keywords:methyl hesperidin  human serum albumin  interaction  fluorescence spectrometry  infrared spectrometry
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