Self-assembly of highly ordered peptide amphiphile metalloporphyrin arrays

H. Christopher Fry, Jamie M. Garcia, Matthew J. Medina, Ulises M. Ricoy, David J. Gosztola, Maxim P. Nikiforov, Liam C. Palmer, Samuel I. Stupp

Research output: Contribution to journalArticle

66 Citations (Scopus)

Abstract

Long fibers assembled from peptide amphiphiles capable of binding the metalloporphyrin zinc protoporphyrin IX ((PPIX)Zn) have been synthesized. Rational peptide design was employed to generate a peptide, c16-AHL 3K3-CO2H, capable of forming a β-sheet structure that propagates into larger fibrous structures. A porphyrin-binding site, a single histidine, was engineered into the peptide sequence in order to bind (PPIX)Zn to provide photophysical functionality. The resulting system indicates control from the molecular level to the macromolecular level with a high order of porphyrin organization. UV/visible and circular dichroism spectroscopies were employed to detail molecular organization, whereas electron microscopy and atomic force microscopy aided in macromolecular characterization. Preliminary picosecond transient absorption data are also reported. Reduced hemin, (PPIX)FeII, was also employed to highlight the material's versatility and tunability.

Original languageEnglish
Pages (from-to)14646-14649
Number of pages4
JournalJournal of the American Chemical Society
Volume134
Issue number36
DOIs
Publication statusPublished - Sep 12 2012

ASJC Scopus subject areas

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

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    Fry, H. C., Garcia, J. M., Medina, M. J., Ricoy, U. M., Gosztola, D. J., Nikiforov, M. P., Palmer, L. C., & Stupp, S. I. (2012). Self-assembly of highly ordered peptide amphiphile metalloporphyrin arrays. Journal of the American Chemical Society, 134(36), 14646-14649. https://doi.org/10.1021/ja304674d