Literature DB >> 18623227

QCM-D sensitivity to protein adsorption reversibility.

Jacob L Jordan1, Erik J Fernandez.   

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.

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Year:  2008        PMID: 18623227      PMCID: PMC6400063          DOI: 10.1002/bit.21977

Source DB:  PubMed          Journal:  Biotechnol Bioeng        ISSN: 0006-3592            Impact factor:   4.530


  20 in total

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6.  Protein unfolding during reversed-phase chromatography: I. Effect of surface properties and duration of adsorption.

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8.  Directed assembly of PEGylated-peptide coatings for infection-resistant titanium metal.

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  8 in total

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