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Mobility of adsorbed proteins: a Brownian dynamics study
1Department of Chemistry, Duquesne University, Pittsburgh, Pennsylvania 15282 USA. ravi@space1.chemistry.duq.edu
Biophysical Journal
|January 5, 2000
Summary
Brownian dynamics simulations reveal how lysozyme adsorbs onto surfaces. Increased ionic strength enhances surface coverage and clustering, while protein mobility decreases with higher surface coverage.
Area of Science:
- Biophysics
- Surface Science
- Computational Chemistry
Background:
- Protein adsorption on solid surfaces is crucial in various applications, including biomaterials and biosensors.
- Understanding the factors influencing protein adsorption kinetics and structure is essential for controlling surface properties.
Purpose of the Study:
- To investigate the adsorption of lysozyme onto a solid surface using Brownian dynamics simulations.
- To analyze the effects of ionic strength and bulk protein concentration on adsorption kinetics, surface layer structure, and protein mobility.
Main Methods:
- Brownian dynamics simulations were employed to model lysozyme adsorption.
- Proteins were represented as uniformly charged spheres interacting via screened Coulombic and double-layer forces.
- Surface coverage, radial distribution function, and mean square displacement were analyzed.
Main Results:
- High ionic strength shielded Coulombic interactions, increasing surface coverage and promoting clustering.
- Lower bulk protein concentrations also promoted clustering at high ionic strengths.
- Lateral protein mobility decreased with increasing surface coverage.
Conclusions:
- Ionic strength and bulk protein concentration significantly influence lysozyme adsorption behavior.
- Simulation results align with existing theoretical and experimental findings on protein adsorption.
- The study provides insights into controlling protein layer formation and dynamics on surfaces.