Controlled protein adsorption to solid material surfaces is a complex phenomenon and is critically important for many biomedical applications.  Force field (FF) based atomistic simulation can be used as a tool to understand these interactions at the molecular level. Using experimentally measured free energy (FE) of peptide adsorption, the CHARMM FF was evaluated for its ability to represent peptide interactions with surfaces presenting several different organic functional groups. Substantial deviations were observed in FE for several surfaces. To correct this, the CHARMM program was modified to incorporate the use of dual-FF in a single simulation to control interfacial and non-interfacial interactions independently. The non-interfacial interactions were modeled using the standard CHARMM FF. Parameterization of an interfacial FF was performed to correct imbalances found in predicting adsorption FE. Using this approach, interfacial parameters were adjusted to accurately model peptide adsorption without altering the peptide conformational behavior in solution.

Accurate modeling of peptide-surface interactions: Interfacial force field parameterization for organic functional groups

244th National Meeting (2012)

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