CAJ | 학술논문

采用反应条件温和的原子转移自由基聚合法（ATRP），以 N-异丙基丙烯酰胺（NIPAAm）和丙烯酰胺（AAm）为功能单体，以 N-（3-二甲氨基丙基）甲基丙烯酰胺（DMAPMA）为辅助功能单体，制备了以牛血清白蛋白（BSA）和溶菌酶（ Lyz）为双模板蛋白质的表面印迹聚合物（ Bi-MIP）。对印迹过程中辅助功能单体的量进行了考察，结果表明，在单一蛋白质溶液和混合蛋白质溶液中，当DMAPMA为20μL时，制备的Bi-MIP对模板蛋白质BSA和Lyz有较好的吸附容量与选择性。通过静态吸附实验考察了 Bi-MIP的吸附性能，并结合 Langmuir吸附模型得到聚合物对模板蛋白质 BSA和 Lyz的最大吸附容量分别为10.2 mg／g和19.2 mg／g。且该印迹聚合物在实际样品中对模板蛋白质也表现出较强的吸附能力和较高的选择性。该方法将为复杂生物样品中同时对双／多种目标蛋白质的识别提供一种新的途径。
채용반응조건온화적원자전이자유기취합법（ATRP），이 N-이병기병희선알（NIPAAm）화병희선알（AAm）위공능단체，이 N-（3-이갑안기병기）갑기병희선알（DMAPMA）위보조공능단체，제비료이우혈청백단백（BSA）화용균매（ Lyz）위쌍모판단백질적표면인적취합물（ Bi-MIP）。대인적과정중보조공능단체적량진행료고찰，결과표명，재단일단백질용액화혼합단백질용액중，당DMAPMA위20μL시，제비적Bi-MIP대모판단백질BSA화Lyz유교호적흡부용량여선택성。통과정태흡부실험고찰료 Bi-MIP적흡부성능，병결합 Langmuir흡부모형득도취합물대모판단백질 BSA화 Lyz적최대흡부용량분별위10.2 mg／g화19.2 mg／g。차해인적취합물재실제양품중대모판단백질야표현출교강적흡부능력화교고적선택성。해방법장위복잡생물양품중동시대쌍／다충목표단백질적식별제공일충신적도경。
The double template surface-imprinted polymer( Bi-MIP )was synthesized by atom transfer radical polymerization( ATRP)in aqueous media,using bovine serum albumin( BSA) and lysozyme( Lyz)as the template proteins,N-isopropylacrylamide( NIPAAm)and acrylam-ide(AAm)as the monomers and N-[3-(dimethylamino)propyl]-methacrylamide(DMAPMA) as the assistant of basic functional monomer. The ATRP possessed the mild reaction conditions and can be initiated at room temperature without heating and ultraviolet radiations. The prepa-ration conditions of imprinted polymer were optimized,and the content of DMAPMA as the assistant of basic functional monomer was investigated. The results showed that Bi-MIP exhibi-ted the good adsorption capacity and selectivity in single protein solution and in mixed protein solution when the volume of DMAPMA in the preparation process of Bi-MIP was 20 μL. The rebinding capacity of Bi-MIP was evaluated according to adsorption isotherm of the imprinted polymer. The Langmuir adsorption model was employed to describe the isotherms and revealed that Bi-MIP exhibited the maximum rebinding to BSA and Lyz at 10. 2 mg/g and 19. 2 mg/g, respectively. And Bi-MIP had good imprinting effect and adsorption capacity to templates BSA and Lyz from egg white and bovine serum samples. This will provide a new way for specific rec-ognition of the double/multiple target proteins in the complex biological samples.