Crystallographic recognition controls peptide binding for bio-based nanomaterials

Ryan Coppage, Joseph M. Slocik, Beverly D. Briggs, Anatoly I. Frenkel, Hendrik Heinz, Rajesh R. Naik, Marc R. Knecht

Research output: Contribution to journalArticle

78 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)12346-12349
Number of pages4
JournalJournal of the American Chemical Society
Volume133
Issue number32
DOIs
StatePublished - Aug 17 2011

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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    Coppage, R., Slocik, J. M., Briggs, B. D., Frenkel, A. I., Heinz, H., Naik, R. R., & Knecht, M. R. (2011). Crystallographic recognition controls peptide binding for bio-based nanomaterials. Journal of the American Chemical Society, 133(32), 12346-12349. https://doi.org/10.1021/ja203726n