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

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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 × 1) : an extension of GolP-CHARMM. The Journal of Physical Chemistry Part C: Nanomaterials, Interfaces and Hard Matter, Volume 117 (Number 46). pp. 24292-24306. doi:10.1021/jp4061329

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Official URL: http://dx.doi.org/10.1021/jp4061329

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Abstract

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.

Item Type: Journal Article
Subjects: Q Science > QA Mathematics > QA76 Electronic computers. Computer science. Computer software
Q Science > QD Chemistry
Divisions: Faculty of Science, Engineering and Medicine > Science > Chemistry
Faculty of Science, Engineering and Medicine > Science > Centre for Scientific Computing
Library of Congress Subject Headings (LCSH): Gold -- Surfaces, Molecular dynamics -- Computer simulation, Interfaces (Physical sciences), Peptides -- Physiology, Molecular recognition
Journal or Publication Title: The Journal of Physical Chemistry Part C: Nanomaterials, Interfaces and Hard Matter
Publisher: American Chemical Society
ISSN: 1932-7447
Official Date: 2013
Dates:
DateEvent
2013Published
Volume: Volume 117
Number: Number 46
Page Range: pp. 24292-24306
DOI: 10.1021/jp4061329
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Restricted or Subscription Access
Funder: Engineering and Physical Sciences Research Council (EPSRC), Federal High Performance Computing Program (U.S.), Istituto Italiano di Tecnologia (IIT), United States. Air Force. Office of Scientific Research (AFOSR)
Grant number: 1117 (HPC); EP/ I001514/1 (EPSRC); FA9550-12-1- 0226 (AFOSR)

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