Plasma protein adsorption to zwitterionic poly (Carboxybetaine Methacrylate) modified surfaces: Chain chemistry and end-group effects on protein adsorption kinetics, adsorbed amounts and immunoblots

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DOIResolve DOI: http://doi.org/10.1007/s13758-012-0040-z
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TypeArticle
Journal titleBiointerphases
ISSN1934-8630
Volume7
Issue1-Apr
Pages114; # of pages: 14
AbstractProtein-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 endgroups that influence the overall hydrophilicity, thereby, allows a better understanding of these effects towards the protein adsorption for thesematerials. 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. © The Author(s) 2012.
Publication date
LanguageEnglish
AffiliationNational Research Council Canada (NRC-CNRC); National Institute for Nanotechnology (NINT-INNT)
Peer reviewedYes
NPARC number21269348
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Record identifier31d410c9-6d32-46d2-8960-9ad1bfa6a5d4
Record created2013-12-12
Record modified2016-05-09
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