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Synthetic formyl tripeptide chemoattractants: a C α, α ‐dialkylated, amphiphilic glycyl residue at position 1
Author(s) -
Witkowska Renata,
Zabrocki Janusz,
Spisani Susanna,
Sofia Falzarano Maria,
Toniolo Claudio,
Formaggio Fernando
Publication year - 2003
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.461
Subject(s) - tripeptide , chemotaxis , chemistry , diastereomer , residue (chemistry) , stereochemistry , tetrapeptide , lysozyme , amphiphile , superoxide , peptide , receptor , biochemistry , enzyme , organic chemistry , copolymer , polymer
The two diastereomeric tripeptides f‐(S)‐HmMet‐Leu‐Phe‐OMe and f‐(R)‐HmMet‐Leu‐Phe‐OMe, analogues of the prototypical chemoattractant f‐Met‐Leu‐Phe‐OH, were synthesized in solution by classical methods and fully characterized. A conformational study was performed in solution by 1 H‐NMR. Concomitantly, the two peptides were tested for their ability to induce chemotaxis, superoxide anion production and lysozyme secretion from human neutrophils. The conformational and biological data are discussed with regard to the proposed model of the chemotactic receptor on neutrophils. Copyright © 2003 European Peptide Society and John Wiley & Sons, Ltd.