ProMetCS: An Atomistic Force Field for Modeling Protein-Metal Surface Interactions in a Continuum Aqueous Solvent.

Area of Science:

• Computational chemistry
• Biophysics
• Materials science

Background:

• Understanding protein-inorganic surface interactions is crucial for various applications.
• Existing methods often require computationally expensive explicit solvent treatments.
• Atomistic modeling of protein-surface association needs efficient and accurate approaches.

Purpose of the Study:

• To present a physics-based energy model, ProMetCS, for simulating protein-inorganic surface association.
• To model protein interactions with an atomically flat gold (Au(111)) surface in aqueous solvent.
• To develop an efficient computational approach for long-time simulations of protein binding.

Main Methods:

• Developed the ProMetCS model treating solvent as a continuum.
• Modeled protein-gold interactions including van der Waals, chemisorption, electrostatic, and desolvation energies.
• Parametrized desolvation energy using molecular dynamics (MD) simulations at a gold-water interface.
• Employed a grid-based procedure for efficient computation of energy terms.

Main Results:

• The ProMetCS model accurately predicts protein-gold binding energies.
• Calculated potentials of mean force for capped amino acid residues showed good quantitative agreement with explicit MD simulations.
• The model demonstrated correspondence with experimental data on amino acid adhesion properties.

Conclusions:

• The ProMetCS model provides an efficient and accurate method for studying protein-inorganic surface interactions.
• The continuum solvent approach simplifies calculations without significant loss of accuracy for protein-gold systems.
• This model facilitates the study of protein association processes on surfaces.