Abstract
The tripeptide N alpha-carbamoyl-L-methionyl-L-leucyl-L-phenylalanine methyl ester has been synthesized in solution by classical methods and fully characterized. This compound, prepared in order to obtain a deeper insight into the mode of binding at the formyl peptide chemotactic receptor, has been tested for its ability to induce granule enzyme secretion from rabbit peritoneal neutrophils and found to be a complete agonist. These results confirm the hypothesis that a proton on the N alpha-blocking group of the tripeptide forms a hydrogen bond with an acceptor in the binding site.
MeSH terms
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Amino Acid Sequence
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Animals
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Chemotactic Factors / chemical synthesis*
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Chemotactic Factors / chemistry
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Chemotactic Factors / pharmacology
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Cytochalasin B / pharmacology
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Hexosaminidases / metabolism
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Hydrogen Bonding
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In Vitro Techniques
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Molecular Sequence Data
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N-Formylmethionine Leucyl-Phenylalanine / analogs & derivatives*
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N-Formylmethionine Leucyl-Phenylalanine / chemical synthesis
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N-Formylmethionine Leucyl-Phenylalanine / chemistry
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Neutrophils / enzymology
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Neutrophils / metabolism*
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Oligopeptides / chemical synthesis*
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Oligopeptides / chemistry
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Oligopeptides / pharmacology
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Rabbits
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Receptors, Formyl Peptide
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Receptors, Immunologic / metabolism
Substances
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Chemotactic Factors
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Oligopeptides
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Receptors, Formyl Peptide
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Receptors, Immunologic
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N(alpha)-carbamoylmethionyl-leucyl-phenylalanine methyl ester
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Cytochalasin B
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N-Formylmethionine Leucyl-Phenylalanine
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Hexosaminidases