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Multiprotein interactions during surface adsorption: a molecular dynamics study of lysozyme aggregation at a charged
Karina Kubiak-Ossowska1, Paul A Mulheran
1Department of Chemical and Process Engineering, University of Strathclyde, James Weir Building, 75 Montrose Street, Glasgow G1 1XJ, United Kingdom.
The Journal of Physical Chemistry. B
|June 16, 2011
Summary
Protein concentration dictates hen egg white lysozyme behavior. At low concentrations, proteins adsorb then aggregate on surfaces; at high concentrations, they aggregate first, then adsorb nonspecifically.
Area of Science:
- Biophysics
- Materials Science
- Computational Chemistry
Background:
- Understanding protein adsorption is crucial for biomaterial development.
- Hen egg white lysozyme is a model protein for studying adsorption phenomena.
Purpose of the Study:
- To investigate multiprotein adsorption of hen egg white lysozyme on a charged ionic surface.
- To elucidate the influence of protein concentration and mutations on adsorption and aggregation behaviors.
Main Methods:
- Fully atomistic molecular dynamics simulations.
- Simulations conducted over a 100 ns timescale with varying numbers of proteins (2, 3, and 5).
- Analysis of mutated proteins with targeted point mutations at key adsorption sites.
Main Results:
- Observed competing processes of surface adsorption and protein-protein aggregation.
- Low protein concentration: initial isolated adsorption followed by surface reorientation and aggregation.
- High protein concentration: initial aggregation in solution preceding non-specific surface adsorption.
Conclusions:
- Protein concentration is a critical factor governing adsorption and aggregation pathways.
- Identified key residues involved in both protein-surface and protein-protein interactions.
- Provides insights for designing functionalized material systems with controlled protein interactions.
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