Abstract
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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 18917-18924 |
| Number of pages | 8 |
| Journal | Journal of Physical Chemistry C |
| Volume | 120 |
| Issue number | 33 |
| DOIs | |
| State | Published - Aug 25 2016 |
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ASJC Scopus subject areas
- Physical and Theoretical Chemistry
- Electronic, Optical and Magnetic Materials
- Surfaces, Coatings and Films
- Energy(all)
Cite this
Peptide Sequence Effects Control the Single Pot Reduction, Nucleation, and Growth of Au Nanoparticles. / Munro, Catherine J.; Hughes, Zak E.; Walsh, Tiffany R.; Knecht, Marc.
In: Journal of Physical Chemistry C, Vol. 120, No. 33, 25.08.2016, p. 18917-18924.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Peptide Sequence Effects Control the Single Pot Reduction, Nucleation, and Growth of Au Nanoparticles
AU - Munro, Catherine J.
AU - Hughes, Zak E.
AU - Walsh, Tiffany R.
AU - Knecht, Marc
PY - 2016/8/25
Y1 - 2016/8/25
N2 - 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.
AB - 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.
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U2 - 10.1021/acs.jpcc.6b06046
DO - 10.1021/acs.jpcc.6b06046
M3 - Article
AN - SCOPUS:84984655292
VL - 120
SP - 18917
EP - 18924
JO - Journal of Physical Chemistry C
JF - Journal of Physical Chemistry C
SN - 1932-7447
IS - 33
ER -