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利用胃蛋白酶键合的有机聚合物整体柱在电色谱中对手性药物奈福泮的拆分能力，采用前沿分析法同时对奈福泮的两个对映体与牛血清白蛋白（BSA）的相互作用情况进行了考察。经过优化后建立的电色谱条件为：胃蛋白酶修饰的聚（甲基丙烯酸环氧丙酯-乙二醇二甲基丙烯酸酯）毛细管整体柱作为分离通道（32 cm ×75μm，有效长度22 cm），运行缓冲液为 pH 5．5的15 mmol／L 醋酸铵，样品溶剂为 pH 7．4的50 mmol／L 醋酸铵，运行电压为5．0 kV，电压进样10 kV ×6 s，检测波长为215 nm。此时奈福泮两个对映体平台峰彼此完全分离，结合体系中 BSA 对对映体在电色谱中的分离和检测均无影响，测得两个对映体与 BSA 的结合常数分别为443和527 L／mol，结合位点数均为1．0，结合位点为 Sudlow site Ⅱ。“,”A pepsin modified poly (glycidyl methacrylate-ethyleneglycol dimethacrylate)(poly (GMA-EDMA)) capillary monolith (32 cm ×75 μm,22cm effective lenth)was applied in exploring the interaction between nefo-pam enantiomers and bovine serum albumin (BSA),mode of frontal analysis was selected to measure the binding constant,number of binding sites and the location of binding sites of BSA to both nefopam enantiomers.The opti-mal CEC conditions obtained were a running buffer consisted of 15 mmol /L ammonium acetate at pH 5.5,separa-tion voltage 5.0 kV,detection wavelength 215 nm,injection 10 kV ×6 s,solvent of samples consisted of 50 mmol/L ammonium acetate at pH 7.4.The results indicated that the monolith could provide a satisfactory resolution between the two enantiomers plateaus,BSA in the binding system didn′t disturb the separation or determination of nefopam enantiomers in electrochromatography.The frontal analysis demonstrated that BSA has only one binding site with both enantiomers,the binding constants (K)were 443 L/mol and 527 L/mol,respectively,and the dis-placement experiments indicated that binding site of both isomers to BSA molecule was the Sudlow siteⅡ.