The molecular imprinting of magnetic nanoparticles with boric acid affinity for the selective recognition and isolation of glycoproteins. Issue 41 (22nd July 2021)

• Record Type: Journal Article
• Authors: Wang, Bangjin; Duan, Aihong; Xie, Shengming; Zhang, Junhui; Yuan, Liming; Cao, Qiue
• Is Part Of: RSC advances. Volume 11:Issue 41(2021)
• Page Start: 25524
• Page End: 25529
• Publication Date: 2021-07-22
• Subjects: Chemistry -- Periodicals; 540.5
• DOI: 10.1039/d1ra00716e
• Languages: English
• ISSNs: 2046-2069

Abstract

Abstract : A strategy was designed for the preparation of molecular imprinting of magnetic nanoparticles with boric acid affinity (MNPs@MIP), and the resultant MNPs@MIP exhibited excellent selectivity for template glycoproteins. Abstract : A strategy was designed for the molecular imprinting of magnetic nanoparticles with boric acid affinity (MNPs@MIP) which were then used for the selective recognition and isolation of glycoproteins. Fe3 O4 nanoparticles were prepared by a solvothermal method and direct silanization by the condensation polymerization of aminopropyltriethoxysilane (APTES). Subsequently, phenylboric acid was functionalized by reductive amination between 2, 3-difluoro-4-formyl phenylboric acid (DFFPBA) and the amido group. The resultant Fe3 O4 @SiO2 –DFFPBA was then used for the selective adsorption of a glycoprotein template. Finally, a molecularly imprinted layer was covered on the surface nanoparticles by the condensation polymerization of tetraethyl orthosilicate (TEOS). The adsorption capacities of the resultant MNPs@MIP–HRP and MNPs@MIP–OVA to horseradish peroxidase (HRP) or ovalbumin (OVA) were significantly higher than non-imprinted particles (MNPs@NIP). Moreover, the adsorption capacities of MNPs@MIP–HRP and MNPs@MIP–OVA on non-template protein and non-glycoprotein bovine serum albumin (BSA) were significantly lower than those of their respective template proteins, thus indicating that both of the prepared MNPs@MIP exhibited excellent selectivity.