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Luminophore Formation in Various Conformations of Bovine Serum Albumin by Binding of Gold(III)
Published on: August 31, 2018
Cupric ion enhanced molecular imprinting of bovine serum albumin in hydrogel
Sheng-Hua Li1, Jun Wang, Mei-Ping Zhao
1Beijing National Laboratory for Molecular Sciences (BNLMS), Key Laboratory of Bioorganic Chemistry and Molecular Engineering of Ministry of Education, College of Chemistry and Molecular Engineering, Peking University, Beijing, China.
Abstract:
A novel molecularly imprinted hydrogel for bovine serum albumin (BSA) was prepared using cupric ion as the bridge between the template BSA and the functional monomer 4-vinylpyridine. N-Isopropylacrylamide (NIPA) was used as an assistant monomer to provide the stimuli-responsibility of the polymer. The adsorption conditions of BSA on the BSA-Cu(II)-imprinted hydrogel were optimized considering the influences of pH, temperature, and salt concentration. The proteins bound on the imprinted hydrogel can be easily recovered under mild conditions by using 10 mmol/L ethylene diamine tetraacetic acid (EDTA) (pH 7.0) containing 150 mmol/L NaCl as the eluting solution. The imprinting effect and adsorption capacity of the polymer were found to be significantly improved compared to the hydrogel prepared in the absence of cupric ion. The results demonstrated the advantages of using a template-metal ion-monomer coordination system to strengthen the interaction between the protein and monomer. The effects of different metals ions including Zn(II), Ni(II), Co(II), Cd(II), and Al(III) on the recognition ability of the BSA-Cu(II)-imprinted hydrogel were also investigated. The polymer showed high selectivity toward both the template protein and the cupric ion.
