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Crystallographic Recognition Controls Peptide Binding for Bio-Based Nanomaterials

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    Crystallographic Recognition Controls Peptide Binding for Bio-Based Nanomaterials
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    † Department of Chemistry, University of Miami, Coral Gables, Florida 33124, United States
    ‡ Nanostructured and Biological Materials Branch, Air Force Research Laboratory, Wright-Patterson Air Force Base, Ohio 45433-7702, United States
    § Department of Physics, Yeshiva University, New York, New York 10016, United States
    ⊥ Department of Polymer Engineering, University of Akron, Akron, Ohio 44325, United States
    [email protected]; [email protected]
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    Cite this: J. Am. Chem. Soc. 2011, 133, 32, 12346–12349
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    https://doi.org/10.1021/ja203726n
    Published July 21, 2011
    Copyright © 2011 American Chemical Society
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    Abstract

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    The ability to control the size, shape, composition, and activity of nanomaterials presents a formidable challenge. Peptide approaches represent new avenues to achieve such control at the synthetic level; however, the critical interactions at the bio/nano interface that direct such precision remain poorly understood. Here we present evidence to suggest that materials-directing peptides bind at specific time points during Pd nanoparticle (NP) growth, dictated by material crystallinity. As such surfaces are presented, rapid peptide binding occurs, resulting in the stabilization and size control of single-crystal NPs. Such specificity suggests that peptides could be engineered to direct the structure of nanomaterials at the atomic level, thus enhancing their activity.

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    Synthetic and simulation procedures, particle size histograms, control analysis, ζ-potential analysis, CD spectra, and full EXAFS analysis. This material is available free of charge via the Internet at http://pubs.acs.org.

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    Cite this: J. Am. Chem. Soc. 2011, 133, 32, 12346–12349
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