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Chemoenzymatic Synthesis of HIV‐1 gp41 Glycopeptides: Effects of Glycosylation on the Anti‐HIV Activity and α‐Helix Bundle‐Forming Ability of Peptide C34
Author(s) -
Wang LaiXi,
Song Haijing,
Liu Shuwen,
Lu Hong,
Jiang Shibo,
Ni Jiahong,
Li Hengguang
Publication year - 2005
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200400440
Subject(s) - gp41 , ectodomain , glycosylation , chemistry , glycopeptide , glycan , glycoprotein , helix bundle , peptide , oligosaccharide , endoglycosidase , biochemistry , stereochemistry , protein structure , biology , receptor , epitope , antigen , antibiotics , genetics
C34 is a 34‐mer peptide derived from the C‐terminal ectodomain of HIV‐1 envelope glycoprotein, gp41. The C34 region in native gp41 carries a conserved N ‐glycan at Asn637 and the sequence is directly involved in the virus–host membrane fusion, an essential step for HIV‐1 infection. This paper describes the synthesis of glycoforms of C34 which carry a monosaccharide, a disaccharide, and a native oligosaccharide moiety. The synthesis of the glycopeptide which carries a native high‐mannose type N ‐glycan was achieved by a chemoenzymatic approach by using an endoglycosidase‐catalyzed oligosaccharide transfer as the key step. The effects of glycosylation on the inhibitory activity and the helix‐bundle forming ability of C34 were investigated. It was found that glycosylation moderately decreases the anti‐HIV activity of C34 and, in comparison with C34, glyco‐C34 forms less compact six‐helix bundles with the corresponding N‐terminal peptide, N36. This study suggests that conserved glycosylation modulates the anti‐HIV activity and conformations of the gp41 C‐peptide, C34.