Synthesis of proteins by native chemical ligation

Science. 1994 Nov 4;266(5186):776-9. doi: 10.1126/science.7973629.

Abstract

A simple technique has been devised that allows the direct synthesis of native backbone proteins of moderate size. Chemoselective reaction of two unprotected peptide segments gives an initial thioester-linked species. Spontaneous rearrangement of this transient intermediate yields a full-length product with a native peptide bond at the ligation site. The utility of native chemical ligation was demonstrated by the one-step preparation of a cytokine containing multiple disulfides. The polypeptide ligation product was folded and oxidized to form the native disulfide-containing protein molecule. Native chemical ligation is an important step toward the general application of chemistry to proteins.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Humans
  • Interleukin-8 / chemical synthesis*
  • Interleukin-8 / chemistry
  • Molecular Sequence Data
  • Oxidation-Reduction
  • Protein Conformation
  • Protein Folding*
  • Proteins / chemical synthesis*
  • Proteins / chemistry

Substances

  • Interleukin-8
  • Proteins