Probing structural requirements of fMLP receptor: On the size of the hydrophobic pocket corresponding to residue 2 of the tripeptide
✍ Scribed by Susanna Spisani; Serena Traniello; Giorgio Cavicchioni; Fernando Formaggio; Marco Crisma; Dr. Claudio Toniolo
- Publisher
- John Wiley and Sons
- Year
- 2002
- Tongue
- English
- Weight
- 151 KB
- Volume
- 8
- Category
- Article
- ISSN
- 1075-2617
- DOI
- 10.1002/psc.369
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✦ Synopsis
Abstract
The conformationally constrained f‐L‐Met‐Ac~n~c‐L‐Phe‐OMe (n = 4,9–12) tripeptides, analogues of the chemoattractant f‐L‐Met‐L‐Leu‐L‐Phe‐OH, were synthesized in solution by classical methods and fully characterized. These compounds and the published f‐L‐Met‐Xxx‐L‐Phe‐OMe (Xxx = Aib and Ac~n~c where n = 3, 5–8) analogues were compared to determine the combined effect of backbone preferred conformation and side‐chain bulkiness at position 2 on the relation of 3D‐structure to biological activity. A conformational study of all the analogues was performed in solution by FT‐IR absorption and ^1^H‐NMR techniques. In parallel, each peptide was tested for its ability to induce chemotaxis, superoxide anion production and lysozyme secretion from human neutrophils. The biological and conformational data are discussed in relation to the proposed model of the chemotactic receptor on neutrophils, in particular of the hydrophobic pocket accommodating residue 2 of the tripeptide. Copyright © 2002 European Peptide Society and John Wiley & Sons, Ltd.