Biological and conformational studies on analogues of a synthetic peptide enhancing HIV-1 infection

Monica Dettin, Claudia Scarinci, Carlo Zanotto, Rossella Roncon, Anita De Rossi, Carlo Di Bello

Research output: Contribution to journalArticle

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.

Original languageEnglish
Pages (from-to)436-448
Number of pages13
JournalJournal of Peptide Science
Volume4
Issue number7
Publication statusPublished - Nov 1998

Keywords

  • CD
  • FT-IR
  • gp120-CD4 interaction
  • HIV-1
  • Solid-phase peptide synthesis
  • Structure-function studies

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Analytical Chemistry

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    Dettin, M., Scarinci, C., Zanotto, C., Roncon, R., De Rossi, A., & Di Bello, C. (1998). Biological and conformational studies on analogues of a synthetic peptide enhancing HIV-1 infection. Journal of Peptide Science, 4(7), 436-448.