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dc.contributor.authorSultan, A.M.*
dc.contributor.authorWestcott, Z.C.*
dc.contributor.authorHughes, Zak E.*
dc.contributor.authorPalafox-Hernandez, J.P.*
dc.contributor.authorGiesa, T.*
dc.contributor.authorPuddu, V.*
dc.contributor.authorBuehler, M.J.*
dc.contributor.authorPerry, C.C.*
dc.contributor.authorWalsh, T.R.*
dc.date.accessioned2018-05-10T14:43:55Z
dc.date.available2018-05-10T14:43:55Z
dc.date.issued2016-07
dc.identifier.citationSultan AM, Westcott ZC, Hughes ZE et al (2016) Aqueous peptide-TiO2 interfaces: isoenergetic binding via either entropically or enthalpically driven mechanisms. ACS Applied Materials & Interfaces. 8(28): 18620-18630.en_US
dc.identifier.urihttp://hdl.handle.net/10454/15854
dc.descriptionYesen_US
dc.description.abstractA major barrier to the systematic improvement of biomimetic peptide-mediated strategies for the controlled growth of inorganic nanomaterials in environmentally benign conditions lies in the lack of clear conceptual connections between the sequence of the peptide and its surface binding affinity, with binding being facilitated by noncovalent interactions. Peptide conformation, both in the adsorbed and in the nonadsorbed state, is the key relationship that connects peptide-materials binding with peptide sequence. Here, we combine experimental peptide–titania binding characterization with state-of-the-art conformational sampling via molecular simulations to elucidate these structure/binding relationships for two very different titania-binding peptide sequences. The two sequences (Ti-1, QPYLFATDSLIK; Ti-2, GHTHYHAVRTQT) differ in their overall hydropathy, yet via quartz-crystal microbalance measurements and predictions from molecular simulations, we show these sequences both support very similar, strong titania-binding affinities. Our molecular simulations reveal that the two sequences exhibit profoundly different modes of surface binding, with Ti-1 acting as an entropically driven binder while Ti-2 behaves as an enthalpically driven binder. The integrated approach presented here provides a rational basis for peptide sequence engineering to achieve the in situ growth and organization of titania nanostructures in aqueous media and for the design of sequences suitable for a range of technological applications that involve the interface between titania and biomolecules.en_US
dc.description.sponsorshipAFOSR grant FA9550-12-1-0226; AFOSR for funding via FA9550-13-1-0040en_US
dc.language.isoenen_US
dc.rights© 2016 ACS. This document is the Accepted Manuscript version of a Published Work that appeared in final form in ACS Applied Materials & Interfaces, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see http://dx.doi.org/10.1021/acsami.6b05200en_US
dc.subjectPeptidesen_US
dc.subjectTitaniaen_US
dc.subjectAdsorptionen_US
dc.subjectMolecular dynamics simulationsen_US
dc.subjectBio-interfacesen_US
dc.titleAqueous peptide-TiO2 interfaces: isoenergetic binding via either entropically or enthalpically driven mechanismsen_US
dc.status.refereedYesen_US
dc.date.application2016-06-29
dc.typeArticleen_US
dc.type.versionAccepted Manuscripten_US
dc.identifier.doihttps://doi.org/10.1021/acsami.6b05200


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