温度对蛋白和β-环糊精手性固定相拆分对映体的影响  

The Effect of Temperature on the Enantiomeric Resolutions on Albumin and β-Cyclodextrin Chiral Stationary Phases

作　　者：张强[1] 邹汉法[1] 陈小明[1] 汪海林[1] 倪坚毅[1] 张曾子[2] 姚平径[2] 

机构地区：[1]中国科学院大连化学物理研究所国家色谱研究分析中心,辽宁大连116011 [2]大连理工大学化工学院,辽宁大连116012

出　　处：《色谱》2001年第1期9-12,共4页Chinese Journal of Chromatography

基　　金：国家自然科学基金!资助项目 (No .2 972 5 5 12 )

摘　　要：采用三聚氯氰为活化剂分别合成了牛血清白蛋白 (BSA)、人血清白蛋白 (HSA)和 β 环糊精手性固定相 ,研究了温度在色氨酸 ,华法令 ,酮基布洛芬和丹酰化苏氨酸手性拆分中的影响。结果表明 ,在蛋白手性固定相上对映体间的熵变对色氨酸 ,华法令和酮基布洛芬的拆分有很大的影响 ,而丹酰化苏氨酸对映体在 β 环糊精手性固定相上的拆分为典型的焓控过程 ,与蛋白柱有着不同的热力学特性。由于键合方式不同 ,色氨酸在我们合成的BSA手性固定相上的最佳分离温度为 35℃左右 ,而不是文献报道的以戊二醛为活化剂的 2 4℃。The effect of column temperature on enantiomeric resolutions of tryptophan, warfarin and ketoprofen was investigated on bovine and human serum albumin (BSA and HSA) stationary phases, which were synthesized with s triazine as the activator. It was observed that the entropy change made a great contribution to the separation of those enantiomers on albumin chiral stationary phases The column temperature for the maximal resolution of tryptophan on the BSA stationary phase prepared by this method was about 35 ℃, which was not 24 ℃ as reported for the BSA stationary phase synthesized with glutaric dialdehyde as the activator This results may come from the different conformation of the immobilized BSA and HSA due to the different coupling methods used On the other hand, it was indicated that the resolution of enantiomers on β CD chiral stationary phase was mainly contributed from the change of enthalpy, which means the resolution of chiral solutes on albumin and β CD stationary phases has different thermodynamic behaviors

关 键 词：蛋白固定相 β-环糊精固定相 热力学 手性拆分 温度 色氨酸 华法令 酮基布洛芬 丹酰化苏氨酸 

分 类 号：O658[理学—分析化学]