Site-specific protein labelling and immobilization mediated by microbial transglutaminase

Chem Commun (Camb). 2014 Jun 25;50(50):6604-6. doi: 10.1039/c4cc00994k.

Abstract

Microbial transglutaminase (mTG) shows broad substrate specificity that is amenable to in vitro bio-conjugation applications. Herein, test proteins were genetically fused with peptide tags, followed by mTG-mediated propargylation of their reactive Gln residues. The propargylated proteins were subjected to copper-assisted azide-alkyne cycloaddition to demonstrate either fluorescent labelling or immobilization.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alkynes / chemistry
  • Azides / chemistry
  • Catalysis
  • Copper / chemistry
  • Cycloaddition Reaction
  • Enzymes, Immobilized / chemistry*
  • Enzymes, Immobilized / metabolism
  • Glutamine / chemistry*
  • Glutamine / metabolism
  • Oligopeptides / chemistry
  • Pargyline / analogs & derivatives*
  • Pargyline / chemistry
  • Pargyline / metabolism
  • Propylamines / chemistry*
  • Propylamines / metabolism
  • Proteins / chemistry*
  • Proteins / metabolism
  • Streptomycetaceae / enzymology
  • Substrate Specificity
  • Transglutaminases / metabolism*

Substances

  • Alkynes
  • Azides
  • Enzymes, Immobilized
  • Oligopeptides
  • Propylamines
  • Proteins
  • Glutamine
  • propargylamine
  • tyrosyl-alanyl-glycine
  • Copper
  • Pargyline
  • Transglutaminases