Synthetic multivalent V3 glycopeptides display enhanced recognition by glycan-dependent HIV-1 broadly neutralizing antibodies

Chem Commun (Camb). 2017 May 14;53(39):5453-5456. doi: 10.1039/c7cc02059g. Epub 2017 May 3.


We describe here the synthesis of novel multivalent HIV V3 domain glycopeptides and their binding to broadly neutralizing antibodies PGT128 and 10-1074. Our binding data reveal a distinct mode of antigen recognition by the two antibodies and further suggest that multivalent glycopeptides could mimic the neutralizing epitopes more efficiently than the monomeric glycopeptide.

MeSH terms

  • Antibody Specificity
  • Glycopeptides*
  • HIV Antibodies / physiology*
  • HIV Envelope Protein gp120 / chemical synthesis*
  • HIV-1 / physiology*
  • Peptide Fragments / chemical synthesis*
  • Polysaccharides / chemistry
  • Polysaccharides / metabolism*
  • Protein Binding


  • Glycopeptides
  • HIV Antibodies
  • HIV Envelope Protein gp120
  • HIV envelope protein gp120 (305-321)
  • Peptide Fragments
  • Polysaccharides