title: Parameterization of an interfacial force field for accurate representation of peptide adsorption free energy on high-density polyethylene.
abstract: Interfacial force field (IFF) parameters for use with the CHARMM force field have been developed for interactions between peptides and high-density polyethylene (HDPE). Parameterization of the IFF was performed to achieve agreement between experimental and calculated adsorption free energies of small TGTG-X-GTGT host-guest peptides (T = threonine, G = glycine, and X = variable amino-acid residue) on HDPE, with ±0.5 kcal/mol agreement. This IFF parameter set consists of tuned nonbonded parameters (i.e., partial charges and Lennard-Jones parameters) for use with an in-house-modified CHARMM molecular dynamic program that enables the use of an independent set of force field parameters to control molecular behavior at a solid-liquid interface. The R correlation coefficient between the simulated and experimental peptide adsorption free energies increased from 0.00 for the standard CHARMM force field parameters to 0.88 for the tuned IFF parameters. Subsequent studies are planned to apply the tuned IFF parameter set for the simulation of protein adsorption behavior on an HDPE surface for comparison with experimental values of adsorbed protein orientation and conformation.
authors.affiliation: Department of Bioengineering, 501 Rhodes Engineering Research Center, Clemson University, Clemson, South Carolina 29634.
authors.forename: Tigran M
authors.initials: TM
authors.lastname: Abramyan
authors.affiliation: Department of Bioengineering, 501 Rhodes Engineering Research Center, Clemson University, Clemson, South Carolina 29634.
authors.forename: James A
authors.initials: JA
authors.lastname: Snyder
authors.affiliation: Department of Bioengineering, 501 Rhodes Engineering Research Center, Clemson University, Clemson, South Carolina 29634.
authors.forename: Jeremy A
authors.initials: JA
authors.lastname: Yancey
authors.affiliation: Department of Bioengineering, 501 Rhodes Engineering Research Center, Clemson University, Clemson, South Carolina 29634.
authors.forename: Aby A
authors.initials: AA
authors.lastname: Thyparambil
authors.affiliation: Department of Bioengineering, 501 Rhodes Engineering Research Center, Clemson University, Clemson, South Carolina 29634.
authors.forename: Yang
authors.initials: Y
authors.lastname: Wei
authors.affiliation: Department of Chemistry, 369 Hunter Laboratories, Clemson University, Clemson, South Carolina 29634.
authors.forename: Steven J
authors.initials: SJ
authors.lastname: Stuart
authors.affiliation: Department of Bioengineering, 501 Rhodes Engineering Research Center, Clemson University, Clemson, South Carolina 29634.
authors.forename: Robert A
authors.initials: RA
authors.lastname: Latour
mesh_terms: D000327:Adsorption; D056004:Molecular Dynamics Simulation; D010455:Peptides / Q000737:chemistry*; D020959:Polyethylene / Q000737:chemistry*; D011485:Protein Binding; D013500:Surface Tension
chemical_list: D010455:Peptides; D020959:Polyethylene
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