A hydrophilic residue at position 2 can improve specific biological responses in fMLP-OMe analogs.
The peptides for-Met-Ser-Phe-OMe 1, for-Met-Cys-Phe-OMe 2, for-Met-Lys-Phe-OMe 3, and for-Met-Tyr-Phe-OMe 4 were synthesized in order to investigate the importance of a hydrophilic side-chain on the residue at position 2 on biological activities of human neutrophils. Our results seem to highlight that this type of substitution does not facilitate good chemotaxis, although it elicits both superoxide anion production and particularly lysozyme release, in some cases even more potent than the parent fMLP-OMe, if the hydrophilicity is associated with steric hindrance.
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Department of Pharmaceutical Sciences, University of Ferrara, Ferrara, Italy. g5z@dns.unife.it
Spisani
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D019943:Amino Acid Substitution; D002633:Chemotaxis / Q000187:drug effects / Q000502:physiology; D006801:Humans; D066298:In Vitro Techniques; D009113:Muramidase / Q000187:drug effects* / Q000378:metabolism; D009240:N-Formylmethionine Leucyl-Phenylalanine / Q000031:analogs & derivatives* / Q000737:chemistry* / Q000494:pharmacology; D009504:Neutrophils / Q000187:drug effects / Q000502:physiology; D009842:Oligopeptides / Q000138:chemical synthesis / Q000737:chemistry* / Q000494:pharmacology*; D013481:Superoxides / Q000819:agonists*
D009842:Oligopeptides; D013481:Superoxides; D009240:N-Formylmethionine Leucyl-Phenylalanine; C042932:formylmethionyl-leucyl-phenylalanine methyl ester; D009113:Muramidase