Peptide sequence effects control the single pot reduction, nucleation, and growth of Au nanoparticles

Munro, Catherine J., Hughes, Zak E., Walsh, Tiffany R. and Knecht, Marc R. 2016, Peptide sequence effects control the single pot reduction, nucleation, and growth of Au nanoparticles, Journal of physical chemistry c, vol. 120, no. 33, pp. 18917-18924, doi: 10.1021/acs.jpcc.6b06046.

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Title Peptide sequence effects control the single pot reduction, nucleation, and growth of Au nanoparticles
Author(s) Munro, Catherine J.
Hughes, Zak E.ORCID iD for Hughes, Zak E. orcid.org/0000-0003-2166-9822
Walsh, Tiffany R.ORCID iD for Walsh, Tiffany R. orcid.org/0000-0002-0233-9484
Knecht, Marc R.
Journal name Journal of physical chemistry c
Volume number 120
Issue number 33
Start page 18917
End page 18924
Total pages 8
Publisher ACS Publications
Place of publication Washington, D.C.
Publication date 2016
ISSN 1932-7447
1932-7455
Keyword(s) Science & Technology
Physical Sciences
Technology
Chemistry, Physical
Nanoscience & Nanotechnology
Materials Science, Multidisciplinary
Chemistry
Science & Technology - Other Topics
Materials Science
Summary Peptides have demonstrated unique capabilities to fabricate inorganic nanomaterials of numerous compositions through noncovalent binding of the growing surface in solution. In this contribution, we demonstrate that these biomolecules can control all facets of Au nanoparticle fabrication, including Au3+ reduction, without the use of secondary reagents. In this regard using the AuBP1 peptide, the N-terminal tryptophan residue is responsible for driving Au3+ reduction to generate Au nanoparticles passivated by the oxidized peptide in solution, where localized residue context effects control the reducing strength of the biomolecule. The process was fully monitored by both time-resolved monitoring of the growth of the localized surface plasmon resonance and transmission electron microscopy. Nanoparticle growth occurs by a unique disaggregation of nanoparticle aggregates in solution. Computational modeling demonstrated that the oxidized residue of the peptide sequence does not impact the biomolecule's ability to bind the inorganic surface, as compared to the parent peptide, confirming that the biomolecule can be exploited for all steps in the nanoparticle fabrication process. Overall, these results expand the utility of peptides for the fabrication of inorganic nanomaterials, more strongly mimicking their use in nature via biomineralization processes. Furthermore, these capabilities enhance the simplicity of nanoparticle production and could find rapid use in the generation of complex multicomponent materials or nanoparticle assembly.
Language eng
DOI 10.1021/acs.jpcc.6b06046
Field of Research 100708 Nanomaterials
100703 Nanobiotechnology
030704 Statistical Mechanics in Chemistry
091202 Composite and Hybrid Materials
Socio Economic Objective 970109 Expanding Knowledge in Engineering
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:30086160

Document type: Journal Article
Collections: Institute for Frontier Materials
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