Postligation-desulfurization: a general approach for chemical protein synthesis

Top Curr Chem. 2015:363:57-101. doi: 10.1007/128_2014_594.

Abstract

Native chemical ligation, involving regioselective and chemoselective coupling of two unprotected peptide segments, enabled the synthesis of polypeptide with more than 200 amino acids. However, cysteine was indispensable in this synthetic technique in its initial format, which limited its further application. Thus, considerable effort has been put into breaking the restriction of cysteine-containing ligation. As a consequence, postligation-desulfurization, concerning thiol-mediated ligation followed by desulfurization, was developed. This review describes the development and recent progress on the chemical synthesis of peptides and proteins encompassing postligation-desulfurization at alanine, valine, lysine, threonine, leucine, proline, arginine, aspartic acid, glutamate, phenylalanine, glutamine, and tryptophan.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Protein Binding
  • Protein Conformation
  • Proteins / chemical synthesis*
  • Proteins / chemistry

Substances

  • Proteins