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QCM-D sensitivity to protein adsorption reversibility
Jacob L Jordan1, Erik J Fernandez
1Department of Chemical Engineering, University of Virginia, 102 Engineers' Way, Charlottesville, Virginia 22904-4741, USA.
Biotechnology and Bioengineering
|July 16, 2008
Summary
Quartz crystal microbalance with dissipative monitoring (QCM-D) revealed protein adsorption reversibility and viscoelastic properties. Specific dissipation correlated with ribonuclease A adsorption reversibility, suggesting structural changes in adsorbed proteins.
Area of Science:
- Biophysics
- Surface Science
- Protein Chemistry
Background:
- Proteins can unfold and denature when interacting with hydrophobic surfaces.
- Understanding protein adsorption is crucial for biomaterial design and diagnostics.
Purpose of the Study:
- To investigate the adsorption reversibility and viscoelastic properties of ribonuclease A on hydrophobic self-assembled monolayers.
- To explore the relationship between protein structure and adsorption behavior.
Main Methods:
- Utilized quartz crystal microbalance with dissipative monitoring (QCM-D) to measure adsorption and viscoelasticity.
- Systematically varied protein concentration, adsorption time, and salt concentration.
Main Results:
- Adsorption reversibility of ribonuclease A increased with higher protein concentrations, shorter adsorption times, and lower ammonium sulfate concentrations.
- A new metric, specific dissipation, was introduced to quantify layer rigidity normalized for adsorbed protein.
- Specific dissipation showed a strong correlation with the observed adsorption reversibility.
Conclusions:
- Specific dissipation may serve as an indicator of structural changes in adsorbed proteins.
- The findings provide insights into protein-surface interactions and the factors influencing protein stability on hydrophobic interfaces.
