Protein-templated peptide ligation

Angew Chem Int Ed Engl. 2014 Apr 22;53(17):4337-40. doi: 10.1002/anie.201400681. Epub 2014 Mar 18.

Abstract

Molecular templates bind particular reactants, thereby increasing their effective concentrations and accelerating the corresponding reaction. This concept has been successfully applied to a number of chemical problems with a strong focus on nucleic acid templated reactions. We present the first protein-templated reaction that allows N-terminal linkage of two peptides. In the presence of a protein template, ligation reactions were accelerated by more than three orders of magnitude. The templated reaction is highly selective and proved its robustness in a protein-labeling reaction that was performed in crude cell lysate.

Keywords: bioorthogonal reactions; peptide ligation; protein modification; solid-phase peptide synthesis; templated reactions.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • CREB-Binding Protein / metabolism*
  • HSP70 Heat-Shock Proteins / chemistry*
  • HSP70 Heat-Shock Proteins / metabolism
  • Humans
  • Magnetic Resonance Spectroscopy
  • Molecular Structure
  • Myeloid-Lymphoid Leukemia Protein / metabolism*
  • Peptide Fragments / metabolism*
  • Protein Conformation
  • Protein Interaction Domains and Motifs

Substances

  • HSP70 Heat-Shock Proteins
  • Peptide Fragments
  • Myeloid-Lymphoid Leukemia Protein
  • CREB-Binding Protein