The ββα fold of zinc finger proteins as a "natural" protecting group. Chemoselective synthesis of a DNA-binding zinc finger derivative

Chem Commun (Camb). 2014 Mar 4;50(18):2258-60. doi: 10.1039/c3cc47599a. Epub 2014 Jan 13.

Abstract

We report the selective modification of cysteine residues engineered in peptides that have two additional cysteine residues as part of a Cys2His2 zinc finger motif. The chemoselective modification is achieved, thanks to the protecting effect exerted by the zinc cation upon coordination with the native cysteines and histidines of the zinc-finger fold. The strategy allows a straightforward synthesis of DNA binding zinc finger constructs.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • Chromatography, High Pressure Liquid
  • Cysteine / chemistry*
  • DNA / chemistry*
  • Histidine / chemistry*
  • Molecular Structure
  • Protein Engineering
  • Protein Folding
  • Zinc Fingers*

Substances

  • Histidine
  • DNA
  • Cysteine