Facile synthesis of hairy core–shell structured magnetic polymer submicrospheres and their adsorption of bovine serum albumin

• Published in: Journal of colloid and interface science 2015-05, Vol.445, p.9-15
• Main Authors: Yan, Xianming, Kong, Juan, Yang, Chongchong, Fu, Guoqi
• Format: Article
• Language: English
• Subjects: Adsorption; Animals; Benzene Derivatives - chemical synthesis; Benzene Derivatives - chemistry; Binding; Cattle; Chemical Precipitation; Distillation–precipitation polymerization; Ferrosoferric Oxide - chemistry; Hairy core–shell structure; Magnetic Phenomena; Magnetic polymer microspheres; Magnets - chemistry; Methacrylates - chemical synthesis; Methacrylates - chemistry; Microspheres; Nylons - chemical synthesis; Nylons - chemistry; Polymerization; Protein adsorption; Proteins; Serum albumin; Serum Albumin, Bovine - chemistry; Shells; Styrenes - chemical synthesis; Styrenes - chemistry; Surface chemistry; Surface-initiated atom transfer radical polymerization
• ISSN: 0021-9797; 1095-7103
• DOI: 10.1016/j.jcis.2014.12.022

[Display omitted] Highly magnetic polymer submicrospheres with a hairy core–shell structure were facilely synthesized by combining distillation–precipitation polymerization (DPP) with subsequent surface-initiated atom transfer radical polymerization (SI-ATRP), and then investigated for protein adsorption. A robust polymer shell consisting of poly(divinylbenzene-co-chloromethylstyrene) (P(DVB-co-CMS)) was coated on superparamagnetic submicrometer-sized magnetite colloid nanocrystal clusters (MCNCs) via DPP. With the benzyl chloride groups on the shell as initiator, poly(2-(dimethylamino) ethyl methacrylate) (PDMAEMA) hairs were grafted by SI-ATRP approach. The resulting hairy core–shell structured Fe3O4@ P(DVB-co-CMS)–PDMAEMA microspheres showed pH- and temperature-sensitivity, and high-magnetization. The composite microspheres were further investigated for adsorption of a typical acidic protein, i.e. bovine serum albumin (BSA). They exhibited a high binding capacity up to over 660mg/g (corresponding to 158 DMAEMA monomer units cooperating for binding one BSA molecule) and could rapidly reach binding equilibrium within 5min. Moreover, the adsorption of BSA was found to be remarkably dependent on the pH and salt concentration of the protein solutions, and the bound protein could be quantitatively desorbed by washing with a medium with lowered pH or raised salt concentration.