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    QCM-D sensitivity to protein adsorption reversibility

    Year: 2008

    Journal: Biotechnology and Bioengineering 2008, Volume 101 Issue 4, Pages 837 - 842, 20100827

    Authors: Jordan J.L. *, Fernandez E.J.

    Last authors: Erik J. Fernandez

    Organizations: Department of Chemical Engineering, University of Virginia, 102 Engineers Way, Charlottesville, Virginia 22904-4741; telephone: 434-924-1351; fax: 434-982-2658

    Country: USA, US, United States of America

    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. Biotechnol. Bioeng. 2008;101: 837-842. © 2008 Wiley Periodicals, Inc.