Development and application of serine/threonine ligation for synthetic protein chemistry

Org Biomol Chem. 2014 Jun 21;12(23):3768-73. doi: 10.1039/c4ob00392f.

Abstract

Chemical synthesis of proteins, especially those with post-translational modifications, has offered new opportunities to study the protein structure-function relationship. In the past four years, we have developed the serine/threonine ligation (STL), which involves the chemoselective reaction between peptide salicylaldehyde esters and peptides with N-terminal serine or threonine. The method has been successfully applied to the synthesis of both linear and cyclic peptides/proteins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acid Anhydride Hydrolases / metabolism
  • Acylphosphatase
  • Amino Acid Sequence
  • Chemistry Techniques, Synthetic / methods*
  • Erythrocytes / enzymology
  • Esters / chemistry
  • Molecular Sequence Data
  • Mucin-1 / metabolism
  • Peptides, Cyclic / chemical synthesis
  • Peptides, Cyclic / chemistry
  • Serine / chemical synthesis*
  • Serine / chemistry
  • Threonine / chemical synthesis*
  • Threonine / chemistry

Substances

  • Esters
  • Mucin-1
  • Peptides, Cyclic
  • Threonine
  • Serine
  • Acid Anhydride Hydrolases