Abstract
Protein-surface interactions are crucial to the overall biocompatability of biomaterials, and are thought to be the impetus towards the adverse host responses such as blood coagulation and complement activation. Only a few studies hint at the ultra-low fouling potential of zwitterionic poly(carboxybetaine methacrylate) (PCBMA) grafted surfaces and, of those, very few systematically investigate their non-fouling behavior. In this work, single protein adsorption studies as well as protein adsorption from complex solutions (i.e. human plasma) were used to evaluate the non-fouling potential of PCBMA grafted silica wafers prepared by nitroxide-mediated free radical polymerization. PCBMAs used for surface grafting varied in charge separating spacer groups that influence the overall surface charges, and chain end-groups that influence the overall hydrophilicity, thereby, allows a better understanding of these effects towards the protein adsorption for these materials. In situ ellipsometry was used to quantify the adsorbed layer thickness and adsorption kinetics for the adsorption of four proteins from single protein buffer solutions, viz, lysozyme, α-lactalbumin, human serum albumin and fibrinogen. Total amount of protein adsorbed on surfaces differed as a function of surface properties and protein characteristics. Finally, immunoblots results showed that human plasma protein adsorption to these surfaces resulted, primarily, in the adsorption of human serum albumin, with total protein adsorbed amounts being the lowest for PCBMA-3 (TEMPO). It was apparent that surface charge and chain hydrophilicity directly influenced protein adsorption behavior of PCBMA systems and are promising materials for biomedical applications.
Highlights
Protein adsorption is considered the impetus behind the initiation of multiple host responses [1]
Given the chemistry of these two systems, it was expected that TEMPO surfaces would be more hydrophobic; suggesting that the TEMPO end-groups may minimize their interaction with water by burying within the initiator layer
Surface properties that influence the protein adsorption were studied by using proteins that varied in size and charge along with surfaces possessing various physiochemical properties
Summary
Protein adsorption is considered the impetus behind the initiation of multiple host responses [1]. A complex process, it’s driven by various forces that exist between surfaces and proteins in solution. Adsorbed proteins obfuscate the underlying engineered interface [2]. Surfaces that can inhibit or prevent protein adsorption in order to improve biomaterial hemocompatibility, as well as allow for engineered interfaces to directly interact with tissue, are actively being sought [3,4,5,6]. Grafting functional polymers is a common surface modification method that may largely suppress protein adsorption and provide improved hemocompatibility, low toxicity, nonimmunogenicity and high water content [7,8,9,10,11,12,13]. Most systems have limited success in preventing long-term biofilm formation [14], long-term material stability [15] and usually suffer in vivo oxidation [16]
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