Using alpha-helical coiled-coils to design nanostructured metalloporphyrin arrays

J Am Chem Soc. 2008 Sep 10;130(36):11921-7. doi: 10.1021/ja800697g. Epub 2008 Aug 19.


We have developed a computational design strategy based on the alpha-helical coiled-coil to generate modular peptide motifs capable of assembling into metalloporphyrin arrays of varying lengths. The current study highlights the extension of a two-metalloporphyrin array to a four-metalloporphyrin array through the incorporation of a coiled-coil repeat unit. Molecular dynamics simulations demonstrate that the initial design evolves rapidly to a stable structure with a small rmsd compared to the original model. Biophysical characterization reveals elongated proteins of the desired length, correct cofactor stoichiometry, and cofactor specificity. The successful extension of the two-porphyrin array demonstrates how this methodology serves as a foundation to create linear assemblies of organized electrically and optically responsive cofactors.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Circular Dichroism
  • Computer Simulation
  • Electron Spin Resonance Spectroscopy
  • Ferric Compounds / chemical synthesis
  • Ferric Compounds / chemistry
  • Metalloporphyrins / chemical synthesis
  • Metalloporphyrins / chemistry*
  • Models, Molecular
  • Molecular Conformation
  • Molecular Sequence Data
  • Molecular Weight
  • Nanostructures / chemistry*
  • Peptides / chemical synthesis
  • Peptides / chemistry*
  • Protein Structure, Secondary
  • Spectrophotometry, Ultraviolet
  • Thermodynamics


  • Ferric Compounds
  • Metalloporphyrins
  • Peptides