Biological and conformational studies on analogues of a synthetic peptide enhancing HIV-1 infection |
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Authors: | Monica Dettin Claudia Scarinci Carlo Zanotto Rossella Roncon Anita De Rossi Carlo Di Bello |
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Abstract: | We have previously demonstrated that a 23-amino acid peptide derived from 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 the 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 entire sequence is required for biological activity and that the sequence 1–18 presents an inhibitory activity. CD and FT-IR absorption data are discussed here in order to identify possible structure-function correlations. © 1998 European Peptide Society and John Wiley & Sons, Ltd. |
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Keywords: | CD FT-IR gp120-CD4 interaction HIV-1 structure-function studies solid-phase peptide synthesis |
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