Preparation and evaluation of mixed-mode resins with tryptophan analogues as functional ligands for human serum albumin separation  

作　　者：Qici Wu Qilei Zhang Shiwen Xu Cheng ong Ge Shanjing Yao Dongqiang Lin 

机构地区：[1]Key Laboratory of Biomass Chemical Engineering of Ministry of Education,College of Chemical and Biological Engineering,Zhejiang University,Hangzhou 310027,China

出　　处：《Chinese Journal of Chemical Engineering》2017年第7期898-905,共8页中国化学工程学报（英文版）

基　　金：Supported by the National Natural Science Foundation of China(21476198,21576233);the International Science&Technology Cooperation Program of China(2015DFG42070)

摘　　要：Five tryptophan analogues with a hydrophobic indole ring and an amino group on each molecule were used as functional ligands of mixed-mode resins for human serum albumin(HSA) purification. Their adsorption performance was evaluated and the effects of p H and salt addition on HSA adsorption were studied. The resins prepared showed typical p H-dependent adsorption and the highest adsorption capacity and affinity were found at pH 5.0for all the resins tested. The saturated adsorption capacity was 138.02 mg·g^(-1)with the tryptaminefunctionalized resin, which significantly decreased at p H below 4.0 due to electrostatic repulsion between ligands and HSA. Moreover, the addition of Na Cl or(NH_4)_2SO_4in media reduced HSA adsorption capacity, although the two salts showed different affecting profiles. The tryptamine-functionalized resin showed the best salt-tolerant performance, and its high adsorption capacity was maintained under high salt concentrations. In addition, the five resins prepared showed good adsorption selectivity for recombinant HSA from Pichia pastoris broth. Molecular docking results between tryptamine and HSA indicated that tryptamine was favorable to bind on Site II(indole-binding site) of HSA.Five tryptophan analogues with a hydrophobic indole ring and an amino group on each molecule were used as functional ligands of mixed-mode resins for human serum albumin（HSA） purification. Their adsorption performance was evaluated and the effects of p H and salt addition on HSA adsorption were studied. The resins prepared showed typical p H-dependent adsorption and the highest adsorption capacity and affinity were found at pH 5.0for all the resins tested. The saturated adsorption capacity was 138.02 mg·g^-1with the tryptaminefunctionalized resin, which significantly decreased at p H below 4.0 due to electrostatic repulsion between ligands and HSA. Moreover, the addition of Na Cl or（NH4）2SO4in media reduced HSA adsorption capacity, although the two salts showed different affecting profiles. The tryptamine-functionalized resin showed the best salt-tolerant performance, and its high adsorption capacity was maintained under high salt concentrations. In addition, the five resins prepared showed good adsorption selectivity for recombinant HSA from Pichia pastoris broth. Molecular docking results between tryptamine and HSA indicated that tryptamine was favorable to bind on Site II（indole-binding site） of HSA.

关 键 词：Adsorption Human serum albumin Mixed-mode chromatography TRYPTAMINE Tryptophan analogue 

分 类 号：O629.73[理学—有机化学] O647.3[理学—化学] O652.6