Glycosylation affects both the three-dimensional structure and antibody binding properties of the HIV-1 IIIB GP120 peptide RP135

Glycosylated analogues of the main neutralizing determinant of gp120 were prepared and their conformations studied by NMR and circular dichroism spectroscopies. RP135, a 24-residue peptide from the HIV-1 IIIB isolate, was glycosylated with N- and O-linked sugars. It was revealed that covalently linking a carbohydrate to a peptide has significant effects on local conformation. The design of ordered and biologically relevant conformations of gp120 could help in designing more effective immunogens for development of HIV-1 vaccines.