Aqueous peptide-TiO2 interfaces: isoenergetic binding via either entropically or enthalpically driven mechanisms

Sultan, Anas M., Westcott, Zayd C., Hughes, Zak E., Palafox-Hernandez, J. Pablo, Giesa, Tristan, Puddu, Valeria, Buehler, Markus J., Perry, Carole C. and Walsh, Tiffany R. 2016, Aqueous peptide-TiO2 interfaces: isoenergetic binding via either entropically or enthalpically driven mechanisms, ACS applied materials & interfaces, vol. 8, no. 28, pp. 18620-18630, doi: 10.1021/acsami.6b05200.

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Title Aqueous peptide-TiO2 interfaces: isoenergetic binding via either entropically or enthalpically driven mechanisms
Author(s) Sultan, Anas M.
Westcott, Zayd C.
Hughes, Zak E.ORCID iD for Hughes, Zak E. orcid.org/0000-0003-2166-9822
Palafox-Hernandez, J. Pablo
Giesa, Tristan
Puddu, Valeria
Buehler, Markus J.
Perry, Carole C.
Walsh, Tiffany R.ORCID iD for Walsh, Tiffany R. orcid.org/0000-0002-0233-9484
Journal name ACS applied materials & interfaces
Volume number 8
Issue number 28
Start page 18620
End page 18630
Total pages 11
Publisher American Chemical Society
Place of publication Washington, D.C.
Publication date 2016
ISSN 1944-8252
Keyword(s) adsorption
biointerfaces
molecular dynamics simulations
peptides
titania
Summary A 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.
Language eng
DOI 10.1021/acsami.6b05200
Field of Research 090301 Biomaterials
030406 Proteins and Peptides
030603 Colloid and Surface Chemistry
030704 Statistical Mechanics in Chemistry
091202 Composite and Hybrid Materials
0904 Chemical Engineering
0303 Macromolecular And Materials Chemistry
0306 Physical Chemistry (Incl. Structural)
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 ©2016, American Chemical Society
Persistent URL http://hdl.handle.net/10536/DRO/DU:30085744

Document type: Journal Article
Collection: Institute for Frontier Materials
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