Conformational features of a synthetic cyclic peptide corresponding to the complete V3 loop of the ELI HIV-1 strain in water

The disulfide bridge closed cyclic peptide corresponding to the whole V3 loop of the envelope protein gp120 of the ELI HIV-1 strain was synthesized and examined bg proton 2D NMR spectroscopy in water. Although the peptide is mainly conformationally flexible, a turn appears to be present at an N-terminal glycosylation site, while in the C-terminal half of the peptide the data point data ard nascent helical structures, Similar conformational preferences in aqueous solution were observed in other V3 loop peptides, especially for the Ile28-Gly30 tripeptide part.