First-principles based force-field for the interaction of proteins with Au(100)(5 x 1): an extension of GolP-CHARMM

Wright, Louise B., Rodger, P. Mark, Walsh, Tiffany R. and Corni, Stefano 2013, First-principles based force-field for the interaction of proteins with Au(100)(5 x 1): an extension of GolP-CHARMM, Journal of physical chemistry C, vol. 117, no. 46, pp. 24292-24306, doi: 10.1021/jp4061329.

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Title First-principles based force-field for the interaction of proteins with Au(100)(5 x 1): an extension of GolP-CHARMM
Author(s) Wright, Louise B.
Rodger, P. Mark
Walsh, Tiffany R.ORCID iD for Walsh, Tiffany R.
Corni, Stefano
Journal name Journal of physical chemistry C
Volume number 117
Issue number 46
Start page 24292
End page 24306
Total pages 15
Publisher American Chemical Society
Place of publication Washington D. C.
Publication date 2013-10-22
ISSN 1932-7447
Summary Noncovalent recognition between peptides and inorganic materials is an established phenomenon. Key to exploiting these interactions in a wide range of materials self-assembly applications would be to harness the facet-selective control of peptide binding onto these materials. Fundamental understanding of what drives facet-selectivity in peptide binding is developing, but as yet is not sufficient to enable design of predictable facet-specific sequences. Computational simulation of the aqueous peptide-gold interface, commonly used to understand the mechanisms driving adsorption at an atomic level, has thus far neglected the role that surface reconstruction might play in facet specificity. Here the polarizable GolP-CHARMM suite of force fields is extended to include the reconstructed Au(100) surface. The force field, compatible with the bio-organic force field CHARMM, is parametrized using first-principles data. Our extended force field is tailored to reproduce the heterogeneity of weak chemisorbing N and S species to specific locations in the Au(100)(5 × 1) surface identified from the first-principles calculations. We apply our new model to predict and compare the three-dimensional structure of liquid water at Au(111), Au(100)(1 × 1), and Au(100)(5 × 1) interfaces. Using molecular dynamics simulations, we predict an increased likelihood for water-mediated peptide adsorption at the aqueous-Au(100)(1 × 1) interface compared with the Au(100)(5 × 1) interface. Therefore, our findings suggest that peptide binding can discriminate between the native and reconstructed Au(100) interfaces and that the role of reconstruction on binding at the Au(100) interface should not be neglected. © 2013 American Chemical Society.
Language eng
DOI 10.1021/jp4061329
Field of Research 030701 Quantum Chemistry
030302 Nanochemistry and Supramolecular Chemistry
030603 Colloid and Surface Chemistry
Socio Economic Objective 970103 Expanding Knowledge in the Chemical Sciences
HERDC Research category C1 Refereed article in a scholarly journal
Copyright notice ©2013, American Chemical Society
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