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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
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 | ||||
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| Subjects: | Q Science > QA Mathematics > QA76 Electronic computers. Computer science. Computer software Q Science > QD Chemistry |
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| Divisions: | Faculty of Science, Engineering and Medicine > Science > Chemistry Faculty of Science, Engineering and Medicine > Science > Centre for Scientific Computing |
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| 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: |
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| 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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