title: Interfacial energetics of protein adsorption from aqueous buffer to surfaces with varying hydrophilicity.
abstract: Adsorption isotherms constructed from time-and-concentration-dependent advancing contact angles thetaa show that the profound biochemical diversity among ten different blood proteins with molecular weight spanning 10-1000 kDa has little discernible effect on the amount adsorbed from aqueous phosphate-buffered saline (PBS) solution after 1 h contact with a particular test surface selected from the full range of observable water wettability (as quantified by PBS adhesion tension tauoa=gammaolv cos thetaoa; where gammaolv is the liquid-vapor interfacial tension and thetaoa is the advancing PBS contact angle). The maximum advancing spreading pressure, Pimaxa, determined from adsorption isotherms decreases systematically with tauoa for methyl-terminated self-assembled monolayers (CH3 SAM, tauo=-15 mN/m), polystyrene spun-coated onto electronic-grade SiOx wafers (PS, tauo=7.2 mN/m), aminopropyltriethoxysilane-treated SiOx surfaces (APTES, tauo = 42 mN/m), and fully water wettable SiOx (tauo=72 mN/m). Likewise, the apparent Gibbs' surface excess [Gammasl-Gammasv], which measures the difference in the amount of protein adsorbed Gamma (mol/cm2) at solid-vapor (SV) and solid-liquid (SL) interfaces, decreases with tauo from maximal values measured on the CH3 SAM surface through zero (no protein adsorption in excess of bulk solution concentration) near tauo=30 mN/m (thetaa=65 degrees). These latter results corroborate the conclusion drawn from independent studies that water is too strongly bound to surfaces with tauo>or=30 mN/m to be displaced by adsorbing protein and that, as a consequence, protein does not accumulate within the interfacial region of such surfaces at concentrations exceeding that of bulk solution ([Gammasl-Gammasv]=0 at tauo=30 mN/m). Results are collectively interpreted to mean that water controls protein adsorption to surfaces and that the mechanism of protein adsorption can be understood from this perspective for a diverse set of proteins with very different amino acid compositions.
authors.affiliation: Department of Materials Science, Materials Research Institute, The Pennsylvania State University, University Park, Pennsylvania 16802, USA.
authors.forename: Paul
authors.initials: P
authors.lastname: Cha
authors.forename: Anandi
authors.initials: A
authors.lastname: Krishnan
authors.forename: Vincent F
authors.initials: VF
authors.lastname: Fiore
authors.forename: Erwin A
authors.initials: EA
authors.lastname: Vogler
mesh_terms: D000327:Adsorption; D001798:Blood Proteins / Q000737:chemistry*; D006801:Humans; D008970:Molecular Weight; D010710:Phosphates / Q000737:chemistry; D012965:Sodium Chloride / Q000737:chemistry; D013499:Surface Properties; D013816:Thermodynamics; D013997:Time Factors; D014867:Water / Q000737:chemistry; D017155:Wettability
chemical_list: D001798:Blood Proteins; D010710:Phosphates; D014867:Water; D012965:Sodium Chloride