Peptide-Modified Surfaces for Binding Carbamylated Proteins from Plasma

Carbamylation of blood proteins is a common post-translational modification that occurs upon kidney dysfunction that is strongly associated with deleterious outcomes for patients treated using hemodialysis. In this study, we focused on the removal of two representative carbamylated plasma proteins, carbamylated albumin (cHSA) and fibrinogen (cFgn), through adsorption onto a surface functionalized with a specific peptide (cH2p1). Surfaces modified with poly(hydroxyethyl methacrylate) (p(HEMA)) were prepared using surface-initiated atom transfer radical polymerization (SI-ATRP) techniques and functionalized with cH2p1. cH2p1-functionalized surfaces showed selective binding toward cHSA and cFgn, compared to their native protein form, with NH-cH2p1 of superior selectivity than CO-cH2p1. The adsorption capacity of carbamylated protein on NH-cH2p1 was maintained in diluted plasma, and ultralow adsorption of native Fgn was observed. Similar to unmodified p(HEMA) surfaces, NH-cH2p1 showed a low platelet adhesion and activation, suggesting that the designed surface does not adversely affect platelets.