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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.

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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 iD for 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 Creative Commons Attribution licence
Persistent URL http://hdl.handle.net/10536/DRO/DU:30077502

Document type: Journal Article
Collections: Institute for Frontier Materials
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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.