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利用荧光光谱法、紫外光谱法并结合计算机模拟技术在分子水平上研究了胡椒碱与人血清白蛋白(human serum albumin HSA)的键合作用.同步荧光及紫外光谱图表明,胡椒碱对HSA微环境有影响.位点竞争试验证明,胡椒碱分子键合在HSA的位点Ⅱ区.通过荧光光谱滴定数据求得不同温度下(300K 310K和318 K)药物与蛋白相互作用的结合常数及结合位点数.分子模拟的结果显示了胡椒碱与HSA的键合区域和键合模式,表明药物与蛋白有较强的键合作用;维持药物与蛋白质的相互作用力主要是疏水用,兼有氢键(位于氨基酸残基Arg 257,Arg 222及Arg218位).通过实验数据计算得到的热力学参数(ΔH0与ΔS0的值分别为原33.11 kJ·mol-1和原18.90 J·mol原1·K-1)确定了胡椒碱与HSA分子的相互作用力类型主要为氢键兼范德华力.
The interaction between piperine and human serum albumin HSA was studied at the molecular level by fluorescence spectroscopy, ultraviolet spectroscopy and computer simulation. The results of synchronous fluorescence and ultraviolet spectroscopy showed that piperine had little effect on the HSA microenvironment Environment.The site competition test showed that piperine was bonded to HSA at site Ⅱ.The binding constant and binding of drug and protein at different temperatures (300K, 310K and 318 K) were determined by fluorescence titration data. Site.The results of molecular simulation showed that the bonding region and bonding mode between piperine and HSA showed that the drug and protein had a strong bonding effect and that the interaction between drug and protein was mainly hydrophobic with hydrogen (Located at amino acid residues Arg 257, Arg 222 and Arg 218) .The thermodynamic parameters (ΔH0 and ΔS0) calculated from the experimental data are the original 33.11 kJ · mol-1 and the original 18.90 J · mol -1 · K- 1) The interaction types between piperine and HSA were identified as hydrogen bond and van der Waals forces.