Structure-activity relationships of cyclic and linear peptide T analogues

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

Research output: Contribution to journalArticle

Abstract

Using the potent cyclic peptide T analog -thr-Thr-Asn-Tyr-Thr-Asp- as parent compound, a series of analogues were synthesized and their potencies in a monocyte chemotaxis assay were compared with those of correspondingly modified linear peptides. Structure-activity relationships observed with cyclic compounds did not always parallel those determined with linear analogues. -Thr-Hse-Asn-Tyr-Thr-Asp- showed the highest affinity to CD4 receptor of monocytes of any peptide thus far studied. It also proved to be highly resistant to degradation by plasma or brain enzymes.

Original languageEnglish
Pages (from-to)447-454
Number of pages8
JournalInternational Journal of Peptide and Protein Research
Volume41
Issue number5
Publication statusPublished - 1993

Keywords

  • Biodegradation
  • Chemotactic activity
  • Homoserine into synthetic peptides
  • Peptide T cyclic analogues

ASJC Scopus subject areas

  • Biochemistry

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    Marastoni, M., Salvadori, S., Balboni, G., Scaranari, V., Spisani, S., Reali, E., Traniello, S., & Tomatis, R. (1993). Structure-activity relationships of cyclic and linear peptide T analogues. International Journal of Peptide and Protein Research, 41(5), 447-454.