fMLP and derivatives
N-formyl-methyonyl peptides are characteristic products of bacteria, they possess strong chemoattractant abilities in eukaryotic systems e.g. in mammalian PMN cells. Modification of the C-terminal part of these peptides could result characteristic changes in chemotactic potency or release of lysosomal enzymes.
Among the set of the tested formyl-peptides only the generally used referent one, fMLP was working as chemoattractant, others were neutral (fMP, fMMM) or chemorepellent (fMLPP, fMV).
Our results suggests that fine, intramolecular physicochemical adjustments are required for the chemoattractant effect of fMLP. Significance of solvent exposed area (SEA) of the C-terminal amino acid residue seems to be significant, low values are preferred over high values, the moderately hydrophobic amino acids (e.g. Val) are advatageous in the formylated dipeptides (Kõhidai et al., Cell Biol. Internat., 27: 695, 2003)
Results gained on the ciliated Tetrahymena proved that FPR (formyl peptide receptor (FPR) linked signaling is a well conserved mechanism in phylogeny.