The Importance of the Peptide Bond at Position 2 in HCO-Met-Leu-Phe-OMe Analogues as shown by Studies on Human Neutrophils
✍ Scribed by Giorgio Cavicchioni; Angela Breveglieri; Marisa Boggian; Gianni Vertuani; Eva Reali; Susanna Spisani
- Publisher
- John Wiley and Sons
- Year
- 1996
- Tongue
- English
- Weight
- 454 KB
- Volume
- 2
- Category
- Article
- ISSN
- 1075-2617
- DOI
- 10.1002/psc.55
No coin nor oath required. For personal study only.
✦ Synopsis
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.