A cyclic peptide T analogue with high chemotactic activity

M. Marastoni, S. Salvadori, G. Balboni, V. Scaranari, S. Spisani, E. Reali, AL Giuliani, R. Tomatis

Research output: Contribution to journalArticlepeer-review

Abstract

Peptide T is an octapeptide (H-Ala-Ser-Thr-Thr-Thr-Asn-Tyr-Thr-OH) based on a consensus sequence that has been identified in HIV proteins. Two conformationally-restricted analogues of peptide T fragment (H-Thr-Thr-Asn-Tyr-Thr-OH) were synthesized by cyclisation of the N-terminal amino group of Thr to the α- or β-carboxyl moiety of Asp introduced at the C-terminus of the peptide. The cyclo Thr-Thr-Asn-Tyr-Thr-Asp(OH) (Cα) showed high in vitro chemotactic activity, whereas the conformational restriction introduced into Thr-Thr-Asn-Tyr-Thr-Asp-OH was incompatible with the CD4 receptor. The cyclic analogue Cα was more active than its ester and the open-chain reference compound H-Thr-Thr-Asn-Tyr-Thr-Asp-OH. It also proved to be highly resistant to degradation by plasma or brain enzymes.

Original languageEnglish
Pages (from-to)383-389
Number of pages7
JournalEuropean Journal of Medicinal Chemistry
Volume27
Issue number4
DOIs
Publication statusPublished - 1992

Keywords

  • biodegradation
  • chemotactic activity
  • peptide T cyclic analogue

ASJC Scopus subject areas

  • Molecular Medicine
  • Organic Chemistry
  • Drug Discovery
  • Pharmaceutical Science

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