Facet selectivity in gold binding peptides: exploiting interfacial water structure Wright, Louise B., Palafox-Hernandez, J. Pablo, Rodger, P. Mark, Corni, Stefano and Walsh, Tiffany R. 2015, Facet selectivity in gold binding peptides: exploiting interfacial water structure, Chemical science, vol. 6, no. 9, pp. 5204-5214, doi: 10.1039/c5sc00399g. Attached Files Name Description MIMEType Size Downloads walsh-facetselectivityin-2015.pdf Published version application/pdf 973.19KB 7 Title Facet selectivity in gold binding peptides: exploiting interfacial water structure Author(s) Wright, Louise B. Palafox-Hernandez, J. Pablo Rodger, P. Mark Corni, Stefano Walsh, Tiffany R. orcid.org/0000-0002-0233-9484 Journal name Chemical science Volume number 6 Issue number 9 Start page 5204 End page 5214 Total pages 11 Publisher Royal Society of Chemistry Place of publication Cambridge, Eng. Publication date 2015 ISSN 2041-6520 2041-6539 Keyword(s) Science & Technology Physical Sciences Chemistry, Multidisciplinary Chemistry EXCHANGE MOLECULAR-DYNAMICS NANOPARTICLE SUPERSTRUCTURES REPLICA-EXCHANGE FREE-ENERGY AU NANOPARTICLES AU(001) SURFACE METAL-SURFACES AMINO-ACIDS ADSORPTION BEHAVIOR DIRECTED SYNTHESIS Summary Peptide sequences that can discriminate between gold facets under aqueous conditions offer a promising route to control the growth and organisation of biomimetically-synthesised gold nanoparticles. Knowledge of the interplay between sequence, conformations and interfacial properties is essential for predictable manipulation of these biointerfaces, but the structural connections between a given peptide sequence and its binding affinity remain unclear, impeding practical advances in the field. These structural insights, at atomic-scale resolution, are not easily accessed with experimental approaches, but can be delivered via molecular simulation. A current unmet challenge lies in forging links between predicted adsorption free energies derived from enhanced sampling simulations with the conformational ensemble of the peptide and the water structure at the surface. To meet this challenge, here we use an in situ combination of Replica Exchange with Solute Tempering with Metadynamics simulations to predict the adsorption free energy of a gold-binding peptide sequence, AuBP1, at the aqueous Au(111), Au(100)(1 × 1) and Au(100)(5 × 1) interfaces. We find adsorption to the Au(111) surface is stronger than to Au(100), irrespective of the reconstruction status of the latter. Our predicted free energies agree with experiment, and correlate with trends in interfacial water structuring. For gold, surface hydration is predicted as a chief determining factor in peptide-surface recognition. Our findings can be used to suggest how shaped seed-nanocrystals of Au, in partnership with AuBP1, could be used to control AuNP nanoparticle morphology. Language eng DOI 10.1039/c5sc00399g Field of Research 030704 Statistical Mechanics in Chemistry 030406 Proteins and Peptides 030603 Colloid and Surface Chemistry 030302 Nanochemistry and Supramolecular Chemistry Socio Economic Objective 970103 Expanding Knowledge in the Chemical Sciences HERDC Research category C1 Refereed article in a scholarly journal ERA Research output type C Journal article Copyright notice ©2015, The Authors Free to Read? Yes Use Rights Persistent URL http://hdl.handle.net/10536/DRO/DU:30077502 Document type: Journal Article Collections: Institute for Frontier Materials Open Access Collection Related Links Link Description Connect to published version Go to link with your DU access privileges     Unless expressly stated otherwise, the copyright for items in DRO is owned by the author, with all rights reserved. Every reasonable effort has been made to ensure that permission has been obtained for items included in DRO. If you believe that your rights have been infringed by this repository, please contact drosupport@deakin.edu.au. Versions Version Filter Type Mon, 31 Aug 2015, 14:04:30 EST Tue, 01 Sep 2015, 05:06:17 EST Wed, 14 Oct 2015, 14:33:04 EST Fri, 11 Mar 2016, 12:40:13 EST Sat, 12 Mar 2016, 05:07:38 EST Wed, 20 Apr 2016, 11:58:43 EST Wed, 20 Apr 2016, 11:59:35 EST Thu, 25 Jan 2018, 13:15:25 EST Thu, 22 Feb 2018, 13:39:29 EST Fri, 07 Sep 2018, 18:14:10 EST Filtered Full Citation counts:   Cited 31 times in TR Web of Science Cited 37 times in Scopus Search Google Scholar Access Statistics: 198 Abstract Views, 8 File Downloads  -  Detailed Statistics Created: Fri, 11 Mar 2016, 12:40:13 EST

Every reasonable effort has been made to ensure that permission has been obtained for items included in DRO. If you believe that your rights have been infringed by this repository, please contact drosupport@deakin.edu.au.