Elucidating the influence of materials-binding peptide sequence on Au surface interactions and colloidal stability of Au nanoparticles

Hughes, Zak E, Nguyen, Michelle A, Li, Yue, Swihart, Mark T, Walsh, Tiffany R and Knecht, Marc R 2017, Elucidating the influence of materials-binding peptide sequence on Au surface interactions and colloidal stability of Au nanoparticles, Nanoscale, vol. 9, no. 1, pp. 421-432, doi: 10.1039/c6nr07890g.

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Title Elucidating the influence of materials-binding peptide sequence on Au surface interactions and colloidal stability of Au nanoparticles
Author(s) Hughes, Zak EORCID iD for Hughes, Zak E orcid.org/0000-0003-2166-9822
Nguyen, Michelle A
Li, Yue
Swihart, Mark T
Walsh, Tiffany RORCID iD for Walsh, Tiffany R orcid.org/0000-0002-0233-9484
Knecht, Marc R
Journal name Nanoscale
Volume number 9
Issue number 1
Start page 421
End page 432
Total pages 12
Publisher Royal Society of Chemistry
Place of publication Cambridge, Eng.
Publication date 2017
ISSN 2040-3372
Keyword(s) materials-binding
Au nanoparticles
Peptide-mediated synthesis
metal surfaces
Science & Technology
Physical Sciences
Chemistry, Multidisciplinary
Nanoscience & Nanotechnology
Materials Science, Multidisciplinary
Physics, Applied
Science & Technology - Other Topics
Materials Science
Gold nanoparticles
Silver nanoparticles
PK(A) values
Summary Peptide-mediated synthesis and assembly of nanostructures opens new routes to functional inorganic/organic hybrid materials. However, understanding of the many factors that influence the interaction of biomolecules, specifically peptides, with metal surfaces remains limited. Understanding of the relationship between peptide sequence and resulting binding affinity and configurations would allow predictive design of peptides to achieve desired peptide/metal interface characteristics. Here, we measured the kinetics and thermodynamics of binding on a Au surface for a series of peptide sequences designed to probe specific sequence and context effects. For example, context effects were explored by making the same mutation at different positions in the peptide and by rearranging the peptide sequence without changing the amino acid content. The degree of peptide-surface contact, predicted from advanced molecular simulations of the surface-adsorbed structures, was consistent with the measured binding constants. In simulations, the ensemble of peptide backbone conformations showed little change with point mutations of the anchor residues that dominate interaction with the surface. Peptide-capped Au nanoparticles were produced using each sequence. Comparison of simulations with nanoparticle synthesis results revealed a correlation between the colloidal stability of the Au nanoparticles and the degree of structural disorder in the surface-adsorbed peptide structures for this family of sequences. These findings suggest new directions in the optimization and design of biomolecules for in situ peptide-based nanoparticle growth, binding, and dispersion in aqueous media.
Language eng
DOI 10.1039/c6nr07890g
Field of Research 100708 Nanomaterials
100706 Nanofabrication, Growth and Self Assembly
030406 Proteins and Peptides
091202 Composite and Hybrid Materials
10 Technology
02 Physical Sciences
03 Chemical Sciences
Socio Economic Objective 970103 Expanding Knowledge in the Chemical Sciences
HERDC Research category C1 Refereed article in a scholarly journal
Copyright notice ©2017, The Royal Society of Chemistry
Persistent URL http://hdl.handle.net/10536/DRO/DU:30090754

Document type: Journal Article
Collections: Institute for Frontier Materials
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