Affinity separation of plasma proteins using a newly synthesized methacrylamidoalanine incorporated porous pHEMA membranes

In this study, we synthesized a novel adsorbent to obtain high protein-adsorption capacity utilizing 2-methacrylamidoalanine (MAAL) containing membrane. Amino acid-ligand MAAL was synthesized by using methacrylochloride and alanine. Then, poly(2-hydroxyethylmethacrylate-co-2-methacrylamidoalanine) [p(HEMA-co-MAAL)] membranes were prepared by UV-initiated photopolymerization of HEMA and MAAL in the presence of an initiator (azobisisobutyronitrile, AIBN). Synthesized MAAL was characterized by nuclear magnetic resonance spectroscopy. p(HEMA-co-MAAL) membranes were characterized by swelling studies, porosimeter, scanning electron microscopy, Fourier transform-infra red spectroscopy, and elemental analysis. These membranes have macropores in the size range 5-10 mum. Different metal ions including Zn(II), Ni(II), Co(II), and Cu(II) were chelated on these membranes. p(HEMA-co-MAAL) were used in the adsorption of human serum albumin (HSA) from aqueous media containing different amounts of albumin (0.1-5.0 mg L-1) and at different pH values (4.0-8.0). The maximum HSA adsorption was observed at pH 5.0. The nonspecific adsorption of HSA on the pHEMA membranes was negligible 0.9 mug cm(-2). MAAL incorporation significantly increased the HSA adsorption (1.76 mg cm(-2)). The HSA adsorption capacities of the metal-incorporated membranes were Greater than that of the p(HEMA-co-MAAL) membranes under the same conditions. Higher HSA adsorption capacity was observed from the human plasma (2.88 mg HSA cm(-2)).