title: QCM-D sensitivity to protein adsorption reversibility.
abstract: Using a quartz crystal microbalance with dissipative monitoring (QCM-D) we have determined the adsorption reversibility and viscoelastic properties of ribonuclease A adsorbed to hydrophobic self-assembled monolayers. Consistent with previous work with proteins unfolding on hydrophobic surfaces, high protein solution concentrations, reduced adsorption times, and low ammonium sulfate concentrations lead to increased adsorption reversibility. Measured rigidity of the protein layers normalized for adsorbed protein amounts, a quantity we term specific dissipation, correlated with adsorption reversibility of ribonuclease A. These results suggest that specific dissipation may be correlated with changes in structure of adsorbed proteins.
authors.affiliation: Department of Chemical Engineering, University of Virginia, 102 Engineers' Way, Charlottesville, Virginia 22904-4741, USA.
authors.forename: Jacob L
authors.initials: JL
authors.lastname: Jordan
authors.forename: Erik J
authors.initials: EJ
authors.lastname: Fernandez
mesh_terms: D000327:Adsorption; D057927:Hydrophobic and Hydrophilic Interactions; D012259:Ribonuclease, Pancreatic / Q000737:chemistry* / Q000493:pharmacokinetics*
chemical_list: D012259:Ribonuclease, Pancreatic