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dc.contributor.authorHughes, Zak E.
dc.contributor.authorNguyen, M.A.
dc.contributor.authorLi, Y.
dc.contributor.authorSwihart, M.T.
dc.contributor.authorWalsh, T.R.
dc.contributor.authorKnecht, M.R.
dc.date.accessioned2018-05-04T14:55:26Z
dc.date.available2018-05-04T14:55:26Z
dc.date.issued2016-12-01
dc.identifier.citationHughes ZE, Nguyen MA, Li Y et al (2016) Elucidating the influence of materials-binding peptide sequence on Au surface interactions and colloidal stability of Au nanoparticles. Nanoscale. 9: 421-432.en_US
dc.identifier.urihttp://hdl.handle.net/10454/15783
dc.descriptionYesen_US
dc.description.abstractPeptide-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.en_US
dc.language.isoenen_US
dc.relation.isreferencedbyhttps://doi.org/10.1039/C6NR07890Gen_US
dc.rights© 2016 RSC. Full-text reproduced in accordance with the publisher’s selfarchiving policy.
dc.subjectBio-nanotechnologyen_US
dc.subjectGold nanoparticlesen_US
dc.subjectMutation effectsen_US
dc.titleElucidating the influence of materials-binding peptide sequence on Au surface interactions and colloidal stability of Au nanoparticlesen_US
dc.status.refereedYesen_US
dc.date.Accepted2016-11-29
dc.date.application2016-12-01
dc.typeArticleen_US
dc.type.versionAccepted manuscripten_US
refterms.dateFOA2018-07-28T03:54:57Z


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