Abstract
The formylpeptides formyl-methionyl-N-methylleucyl-phenylalanine methyl ester [for-Met-(NMe)Leu-Phe-OMe] 1, formyl-methionyl-2-aminotetralin-2-carboxyl-phenylalanine methyl ester [for-Met-Atc-Phe-OMe] 2, formyl-methionyl-1,2,3,4-tetrahydroisoquinoline-3-carboxyl-phenylalanine methyl ester [for-Met-Tic-Phe-OMe] 3 and formyl-methionyl-2-aminoxy-4-methylvaleryl-phenylalanine methyl ester [for-Met-OLeu-Phe-OMe] 4 were synthesized in order to investigate the role of the amide bond at position 2 on biological activities on human neutrophils. Only analogue 2, which keeps the NH group at position 2, was found to retain activity though sterically encumbered.
| Original language | English |
|---|---|
| Pages (from-to) | 135-140 |
| Number of pages | 6 |
| Journal | Journal of Peptide Science |
| Volume | 2 |
| Issue number | 3 |
| Publication status | Published - May 1996 |
Keywords
- Chemotaxis
- Human neutrophils
- Lysozyme release
- N-formylmethionyl peptides
- Superoxide anion generation
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Analytical Chemistry
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Cite this
Cavicchioni, G., Breveglieri, A., Boggian, M., Vertuani, G., Reali, E., & Spisani, S. (1996). The Importance of the peptide bond at position 2 in HCO-Met-Leu-Phe-OMe analogues as shown by studies on human neutrophils. Journal of Peptide Science, 2(3), 135-140.