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 language | English |
|---|---|
| Pages (from-to) | 447-454 |
| Number of pages | 8 |
| Journal | International Journal of Peptide and Protein Research |
| Volume | 41 |
| Issue number | 5 |
| Publication status | Published - 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.