Chemoenzymatic synthesis of glycosylphosphatidylinositol-anchored glycopeptides

Chem Commun (Camb). 2010 Aug 21;46(31):5773-4. doi: 10.1039/c0cc00828a. Epub 2010 Jun 24.

Abstract

MUC1 glycopeptide was efficiently coupled to glycosylphosphatidylinositol (GPI) derivatives by sortase A (SrtA), verifying that SrtA can accept sterically hindered glycopeptide as substrate for ligation with GPIs. This work has established a practical method for the chemoenzymatic synthesis of GPI-linked glycopeptides.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Aminoacyltransferases / metabolism
  • Bacterial Proteins / metabolism
  • Biocatalysis
  • Carbohydrate Sequence
  • Cysteine Endopeptidases / metabolism
  • Glycopeptides / biosynthesis*
  • Glycopeptides / chemistry
  • Glycosylphosphatidylinositols / chemistry*
  • Molecular Sequence Data
  • Mucin-1 / chemistry

Substances

  • Bacterial Proteins
  • Glycopeptides
  • Glycosylphosphatidylinositols
  • Mucin-1
  • Aminoacyltransferases
  • sortase A
  • Cysteine Endopeptidases