Chemoenzymatic synthesis of HIV-1 V3 glycopeptides carrying two N-glycans and effects of glycosylation on the peptide domain.
[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.
Li
Hengguang
H
Institute of Human Virology and Medical Biotechnology Center, University of Maryland Biotechnology Institute, University of Maryland, 725 W. Lombard Street, Baltimore, Maryland 21201, USA.
Li
Bing
B
Song
Haijing
H
Breydo
Leonid
L
Baskakov
Ilia V
IV
Wang
Lai-Xi
LX
D000595:Amino Acid Sequence; D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D006020:Glycopeptides / Q000138:chemical synthesis* / Q000737:chemistry; D006031:Glycosylation; D015699:HIV Envelope Protein gp120 / Q000737:chemistry*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry*; D011134:Polysaccharides / Q000737:chemistry*; D013237:Stereoisomerism
D006020:Glycopeptides; D015699:HIV Envelope Protein gp120; D010446:Peptide Fragments; D011134:Polysaccharides