Chemoenzymatic synthesis of HIV-1 V3 glycopeptides carrying two N-glycans and effects of glycosylation on the peptide domain

J Org Chem. 2005 Nov 25;70(24):9990-6. doi: 10.1021/jo051729z.


[structure: see text] A highly efficient chemoenzymatic synthesis of HIV-1 V3 domain glycopeptides carrying two N-linked core tri- and pentasaccharides was achieved. The synthesis consisted of two key steps: a solid-phase synthesis of the cyclic, 47-mer V3 domain peptide containing two GlcNAc residues and a novel endoglycosidase-catalyzed transglycosylation that simultaneously added two N-glycan moieties to the peptide precursor from the oligosaccharide oxazoline donor substrates. The availability of the synthetic glycopeptides allowed the probing of the effects of glycosylation on the HIV-1 V3 domain. It was demonstrated that glycosylation influenced the global conformations of the V3 domain and provided protection of the V3 domain against protease digestion.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Amino Acid Sequence
  • Carbohydrate Conformation
  • Carbohydrate Sequence
  • Glycopeptides / chemical synthesis*
  • Glycopeptides / chemistry
  • Glycosylation
  • HIV Envelope Protein gp120 / chemistry*
  • Molecular Sequence Data
  • Peptide Fragments / chemistry*
  • Polysaccharides / chemistry*
  • Stereoisomerism


  • Glycopeptides
  • HIV Envelope Protein gp120
  • Peptide Fragments
  • Polysaccharides