Environmentally responsive histidine-carboxylate zipper formation between proteins and nanoparticles

Nanoscale. 2014 Aug 7;6(15):8873-7. doi: 10.1039/c4nr02097a.

Abstract

Interfacing synthetic materials with biomacromolecules provides new systems for biological applications. We report the creation of a reversible multivalent supramolecular "zipper" recognition motif between gold nanoparticles and proteins. In this assembly, carboxylate-functionalized nanoparticles interact strongly with oligohistidine tags. This interaction can be tuned through His-tag length, and offers unique binding profiles based on the pH and electrolyte concentration of the medium.

Publication types

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

MeSH terms

  • Biocompatible Materials / chemistry*
  • Carboxylic Acids / chemistry*
  • Cloning, Molecular
  • Escherichia coli / metabolism
  • Genetic Engineering
  • Gold / chemistry
  • Green Fluorescent Proteins / chemistry
  • Histidine / chemistry*
  • Hydrogen-Ion Concentration
  • Ions
  • Ligands
  • Macromolecular Substances / chemistry
  • Metal Nanoparticles / chemistry
  • Nanoparticles / chemistry*
  • Protein Binding
  • Protein Engineering
  • Proteins / chemistry*
  • Recombinant Proteins / chemistry

Substances

  • Biocompatible Materials
  • Carboxylic Acids
  • Ions
  • Ligands
  • Macromolecular Substances
  • Proteins
  • Recombinant Proteins
  • Green Fluorescent Proteins
  • Histidine
  • Gold