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dc.contributor.authorHughes, Zak E.*
dc.contributor.authorWalsh, T.R.*
dc.date.accessioned2018-08-17T15:43:32Z
dc.date.available2018-08-17T15:43:32Z
dc.date.issued2018-08
dc.identifier.citationHughes ZE and Walsh TR (2018) Distinct differences in peptide adsorption on palladium and gold: introducing a polarizable model for Pd(111). The Journal of Physical Chemistry C. 122(34): 19625-19638.en_US
dc.identifier.urihttp://hdl.handle.net/10454/16543
dc.descriptionYesen_US
dc.description.abstractMaterials-binding peptides offer promising routes to the production of tailored Pd nanomaterials in aqueous media, enabling the optimization of catalytic properties. However, the atomic-scale details needed to make these advances are relatively scarce and challenging to obtain. Molecular simulations can provide key insights into the structure of peptides adsorbed at the aqueous Pd interface, provided that the force-field can appropriately capture the relevant bio-interface interactions. Here, we introduce and apply a new polarizable force field, PdP-CHARMM, for the simulation of biomolecule–Pd binding under aqueous conditions. PdP-CHARMM was parametrized with density functional theory (DFT) calculations, using a process compatible with similar polarizable force-fields created for Ag and Au surfaces, ultimately enabling a direct comparison of peptide binding modes across these metal substrates. As part of our process for developing PdP-CHARMM, we provide an extensive study of the performance of ten different dispersion-inclusive DFT functionals in recovering biomolecule–Pd(111) binding. We use the functional with best all-round performance to create PdP-CHARMM.We then employ PdP-CHARMM and metadynamics simulations to estimate the adsorption free energy for a range of amino acids at the aqueous Pd(111) interface. Our findings suggest that only His and Met favor direct contact with the Pd substrate, which we attribute to a remarkably robust interfacial solvation layering. Replica-exchange with solute tempering molecular dynamics simulations of two experimentally-identified Pd-binding peptides also indicate surface contact to be chiefly mediated by His and Met residues at aqueous Pd(111). Adsorption of these two peptides was also predicted for the Au(111) interface, revealing distinct differences in both the solvation structure and modes of peptide adsorption at the Au and Pd interfaces. We propose that this sharp contrast in peptide binding is largely due to the differences in interfacial solvent structuring.en_US
dc.description.sponsorshipAir Force Office for Scientfi c Research (Grant #FA9550-12-1-0226)en_US
dc.language.isoenen_US
dc.rights© 2018 ACS. This document is the Accepted Manuscript version of a Published Work that appeared in final form in The Journal of Physical Chemistry C, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see https://doi.org/10.1021/acs.jpcc.8b05860.en_US
dc.subjectPeptide adsorptionen_US
dc.subjectPolarizable force fielden_US
dc.subjectPdP-CHARMMen_US
dc.subjectPalladiumen_US
dc.subjectGolden_US
dc.subjectDensity functional theory (DFT)en_US
dc.subjectPeptide bindingen_US
dc.titleDistinct differences in peptide adsorption on palladium and gold: introducing a polarizable model for Pd(111)en_US
dc.status.refereedYesen_US
dc.date.Accepted2018-08-07
dc.date.application2018-08-07
dc.typeArticleen_US
dc.type.versionAccepted Manuscripten_US
dc.identifier.doihttps://doi.org/10.1021/acs.jpcc.8b05860
refterms.dateFOA2018-08-17T15:43:38Z


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