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Selective uptake of different proteins by annealed and quenched cationic spherical polyelectrolyte brushes
Author(s) -
Ye Zhishuang,
Li Li,
Dai Liheng,
Wang Yunwei,
Yang Qingsong,
von Klitzing Regine,
Guo Xuhong
Publication year - 2020
Publication title -
journal of polymer science
Language(s) - English
Resource type - Journals
eISSN - 2642-4169
pISSN - 2642-4150
DOI - 10.1002/pol.20200547
Subject(s) - ionic strength , small angle x ray scattering , polyelectrolyte , adsorption , cationic polymerization , dynamic light scattering , desorption , chemistry , polymer chemistry , methacrylate , chemical engineering , bovine serum albumin , ionic bonding , materials science , scattering , chromatography , ion , polymer , organic chemistry , nanotechnology , aqueous solution , monomer , physics , engineering , nanoparticle , optics
Abstract The selective uptake of bovine serum albumin (BSA) and β‐glucosidase (β‐G) by annealed and quenched cationic spherical polyelectrolyte brushes (SPB) was systematically studied by combining turbidimetric titration, dynamic light scattering and small angle X‐ray scattering (SAXS). These two kinds of SPB consist of a same polystyrene core and a dense shell of poly (2‐aminoethyl methacrylate hydrochloride) (PAEMH) and poly [2‐(methacryloyloxy) ethyl] trimethylammonium chloride (PMAETA), respectively. Results reveal that the adsorption/desorption of proteins on SPB can be easily controlled by changing external conditions (pH and ionic strength). For a particular annealed or quenched SPB, there is a significant difference of the interaction pH regions between the brush and the two proteins, and this difference can be tuned by ionic strength. At low ionic strength, quenched brushes were more suitable for selective adsorption of BSA and β‐G, while annealed brushes performed better at high ionic strength. SAXS analysis demonstrated that volume exclusion effect played a remarkable role in protein uptake by both SPB, and larger proteins were more likely to be adsorbed on the outer layer of the brush. The unique core‐shell structure and controllable chain types make SPB an excellent candidate in selective adsorption/separation of proteins of different sizes.