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    Unusual Reactivity of a Silver Mineralizing Peptide
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    † Department of Chemistry and Biochemistry, University of Colorado, Boulder, Colorado 80309
    ‡ Department of Chemistry, Colorado State University, Fort Collins, Colorado 80523
    * Address correspondence to [email protected]
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    ACS Nano

    Cite this: ACS Nano 2010, 4, 7, 3883–3888
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    https://doi.org/10.1021/nn100630v
    Published June 16, 2010
    Copyright © 2010 American Chemical Society
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    Abstract

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    The ability of peptides selected via phage display to mediate the formation of inorganic nanoparticles is now well established. The atomic-level interactions between the selected peptides and the metal ion precursors are in most instances, however, largely obscure. We identified a new peptide sequence that is capable of mediating the formation of Ag nanoparticles. Surprisingly, nanoparticle formation requires the presence of peptide, HEPES buffer, and light; the absence of any one of these compromises nanoparticle formation. Electrochemical experiments revealed that the peptide binds Ag+ in a 3 Ag+:1 peptide ratio and significantly alters the Ag+ reduction potential. Alanine replacement studies yielded insight into the sequence-function relationships of Ag nanoparticle formation, including the Ag+ coordination sites and the residues necessary for Ag synthesis. In addition, the peptide was found to function when immobilized onto surfaces, and the specific immobilizing concentration could be adjusted to yield either spherical Ag nanoparticles or high aspect ratio nanowires. These studies further illustrate the range of interesting new solid-state chemistries possible using biomolecules.

    Copyright © 2010 American Chemical Society

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    ACS Nano

    Cite this: ACS Nano 2010, 4, 7, 3883–3888
    Click to copy citationCitation copied!
    https://doi.org/10.1021/nn100630v
    Published June 16, 2010
    Copyright © 2010 American Chemical Society
    Request reuse permissions

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