Comparison of implicit solvent models for the simulation of protein-surface interactions

Area of Science:

• Computational chemistry
• Biophysics
• Materials science

Background:

• Molecular simulations offer atomistic insights into protein-surface interactions.
• Implicit solvation models enhance simulation efficiency but may lack accuracy for protein-surface systems.
• Existing models were developed for proteins in solution, not for interactions with synthetic materials.

Purpose of the Study:

• To evaluate implicit solvation models for peptide-surface interactions.
• To compare empirical force field models (ACE, ASP, EEF1, RDIE) with DFT/SCRF.
• To assess model suitability for protein-material interface simulations.

Main Methods:

• Calculated free energy changes for peptide-surface interactions using four implicit solvation models.
• Employed the CHARMM 19 force field with ACE, ASP, EEF1, and RDIE models.
• Validated results against density functional theory (DFT) with self-consistent reaction field (SCRF).

Main Results:

• Different implicit solvation models predicted distinct behaviors.
• The ACE model demonstrated the best agreement with DFT/SCRF calculations.
• Identified limitations of the ACE model for this specific application.

Conclusions:

• ACE is a promising implicit solvation model for protein-surface interactions.
• Further parameter refinement is needed for enhanced accuracy.
• This study provides a foundation for improving implicit solvent models in biomaterial simulations.