posted on 2021-10-13, 17:42authored byYuhao Ma, Narges Hadjesfandiari, Michael Doschak, Dana Devine, Marcello Tonelli, Larry Unsworth
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.