BIOLOGICAL AND CONFORMATIONAL STUDIES ON ANALOGS OF A SYNTHETIC PEPTIDE ENHANCING HIV-1 INFECTION

We have previously demonstrated that a 23-amino acid peptide derived f rom the V3 loop of the surface glycoprotein of the HIV-1 strain MN is able to bind CD4 and to enhance HIV-1 infection. Further studies have suggested that the peptide/CD4 interaction induces an increase in both CD4 expression and CD4/gp120 binding affinity. This paper describes t he biological and physico-chemical characterization of three analogues of reduced sequence that have been designed in order:to identify the minimum active sequence of this peptide corresponding to the MN-HIV-1 principal neutralizing domain. Biological studies indicate that the en tire sequence is required for biological activity and that the sequenc e 1-18 presents an inhibitory activity. CD and FT-IR absorption data a re discussed here in order to identify possible structure-function cor relations. (C) 1998 European Peptide Society and John Wiley & Sons, Lt d.