Premium
QCM‐D sensitivity to protein adsorption reversibility
Author(s) -
Jordan Jacob L.,
Fernandez Erik J.
Publication year - 2008
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.21977
Subject(s) - quartz crystal microbalance , adsorption , chemistry , monolayer , protein adsorption , ribonuclease , hydrophobic effect , chromatography , dissipation , chemical engineering , organic chemistry , biochemistry , thermodynamics , rna , physics , engineering , gene
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.