Protein adsorption on polyanion/polycation layer-by-layer assembled polyelectrolyte films

Abstract

As layer-by-layer self-assembly deposition (LbL) is a versatile technique for surface modification, protein adsorption on the LbL modified glass is evaluated in this study. At the beginning, glass slides was silanized by 3-aminopropyltriethoxysilane (APTES). Sodium alginate (Alg), poly(γ-glutamic acid) (PGA) and poly(aspartic acid) (PAsp) were selected as polyanion electrolytes and chitosan (CS) was used as the polycation electrolyte. Both polyanion and polycation electrolytes alternately deposited on the silanized glass slide surface by the LbL technique to get three different polyanion/chitosan series of LbL films ([Alg/CS], [PGA/CS], and [PAsp/CS]). Three kinds of kinetic model including pseudo-first-order, second-order kinetic and intraparticle diffusion model were used to evaluate the adsorption of albumin on the three different polyanion/chitosan series of LbL films. It is found that the adsorption of albumin on the polyanion/chitosan series of LbL films can be described well with the pseudo-second-order kinetic mechanism. To make sure if the pseudo-second-order kinetic mechanism of protein adsorbed on the other polyanion/polycation LbL films is also suitable, poly(allylamine hydrochloride) (PAH) and poly(L-lysine) (PLL) are used as two other polycations. The [polyanion/PAH] and [polyanion/PLL] series of LbL films were prepared with the same LbL technique for albumin, fibrinogen, and fibronectin adsorption. From the results, it is found that albumin, fibrinogen, and fibronectin adsorption on the various polyanion/polycation LbL films can be described well with the pseudo-second-order kinetic mechanism. The protein adsorbed at equilibrium and rate constant of protein adsorbed on the various LbL films can be determined.