Sortase-catalyzed peptide-glycosylphosphatidylinositol analogue ligation

J Am Chem Soc. 2009 Jul 29;131(29):9878-9. doi: 10.1021/ja903231v.

Abstract

It is demonstrated that sortase A (SrtA) can catalyze efficient coupling of peptides to GPI analogues with a glycine residue attached to the phosphoethanolamine moiety at the nonreducing end to form GPI-linked peptides. This represents the first chemoenzymatic synthesis of GPI-peptide conjugates and is a proof-of-concept for the potential application of SrtA to the synthesis of more complex GPI-anchored peptides/glycopeptides and GPI-anchored proteins/glycoproteins.

Publication types

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

MeSH terms

  • Aminoacyltransferases / metabolism*
  • Bacterial Proteins / metabolism*
  • Biocatalysis
  • Carbohydrate Conformation
  • Cysteine Endopeptidases / metabolism*
  • Glycosylphosphatidylinositols / chemistry
  • Glycosylphosphatidylinositols / metabolism*
  • Molecular Sequence Data
  • Peptides / chemistry
  • Peptides / metabolism*

Substances

  • Bacterial Proteins
  • Glycosylphosphatidylinositols
  • Peptides
  • Aminoacyltransferases
  • sortase A
  • Cysteine Endopeptidases