The design of a specific ligand of HIV gp120

Maria Scarselli, Antonio Facchiano, Giandomenico Russo, Henriette Molinari, Laura Ragona, Lucia Zetta, Neri Niccolai

Research output: Contribution to journalArticle

Abstract

The crystal structure of CD4 suggested that the C/G38 and C/L44 replacements with the consequent cystine bridge formation are compatible with the native structure of that molecular moiety. As the NQGSF sequence, corresponding to the 39-43 fragment of human CD4 protein, was found to be involved in the HIV gp120 interaction, it has been synthesized in a cyclic form by adding two cysteine residues at the amino and carboxy termini. 1H-NMR studies show that the predominant solution conformation of cyclo-[CNQGSFC] is a type II β-turn centred on the NQGS segment. Structural and dynamic properties of the peptide are also analysed in relation to the in vitro activity.

Original languageEnglish
Pages (from-to)383-390
Number of pages8
JournalJournal of Peptide Science
Volume3
Issue number5
Publication statusPublished - Sep 1997

Keywords

  • CD4
  • gp120
  • NMR
  • Peptides
  • Structure

ASJC Scopus subject areas

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

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    Scarselli, M., Facchiano, A., Russo, G., Molinari, H., Ragona, L., Zetta, L., & Niccolai, N. (1997). The design of a specific ligand of HIV gp120. Journal of Peptide Science, 3(5), 383-390.