Metallization of a genetically engineered polypeptide

Macromol Biosci. 2012 Feb;12(2):269-73. doi: 10.1002/mabi.201100245. Epub 2011 Dec 6.

Abstract

Recently, well-ordered biological materials have been exploited to pattern inorganic nanoparticles into linear arrays that are of particular interest for nanoelectronic applications. In this work, a de novo designed E. coli-expressed polypeptide (previously shown to form highly rectilinear, β-sheet-containing structures) operates as a template for divalent metal cations. EDX and TEM analysis verify the attachment of platinum ions to the histidine-rich fibril surface, which was designed specifically to facilitate attachment of chemical moieties. Following chemical reduction, TEM further confirms the formation of localized zero-valent metal aggregates with sub-nanometer interparticle spacing.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Biocompatible Materials / analysis
  • Biocompatible Materials / chemical synthesis*
  • Cations, Divalent / chemistry
  • Escherichia coli
  • Histidine / chemistry
  • Microscopy, Electron, Transmission
  • Molecular Sequence Data
  • Nanotechnology / methods*
  • Peptides / chemistry*
  • Peptides / genetics
  • Platinum / chemistry*
  • Protein Engineering
  • Protein Structure, Secondary
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Spectrometry, X-Ray Emission

Substances

  • Biocompatible Materials
  • Cations, Divalent
  • Peptides
  • Recombinant Proteins
  • Platinum
  • Histidine