The main functions and structural modifications of tripeptide N-formyl-methionyl-leucyl-phenylalanine (fMLP) as a chemotactic factor

• Published in: Pharmazie Vol. 63; no. 11; pp. 779 - 783
• Main Authors: Yang, K. H., Fang, H., Ye, J. S., Gong, J. Z., Wang, J. T., Xu, W. F.
• Format: Journal Article
• Language: English
• Published: Germany Govi-Verlag 01.11.2008
• Subjects: Alopecia - prevention & control; Analgesics - pharmacology; Animals; Anti-Bacterial Agents - pharmacology; Anti-HIV Agents - pharmacology; Antineoplastic Agents - pharmacology; Chemotactic Factors - chemistry; Chemotactic Factors - pharmacology; Humans; N-Formylmethionine Leucyl-Phenylalanine - chemistry; N-Formylmethionine Leucyl-Phenylalanine - pharmacology; Signal Transduction - drug effects; Structure-Activity Relationship
• ISSN: 0031-7144
• DOI: 10.1691/ph.2008.8595

Gram negative bacteria-derived and synthetic N-formyl peptides play a key role in host defense as chemotactic factors for phagocytic leukocytes. The first compound to be identified was N-formyl-methionyl-leucyl-phenylalanine (fMLP) which contains highly potent leukocyte chemoattractant. Natural fMLP was subsequently purified and identified in supernatants of gram negative bacteria. Recently, much more attention has been focused on the human formyl peptide receptor (FPR) and its variant formyl peptide receptor-like 1 (FPRL1) and formyl peptide receptor-like 2 (FPRL2). Chemotactic factors such as fMLP interact with their specific cell surface receptors, which results in multiple biological responses through a G protein-coupled signal pathway. In this review, the functions and structural modifications of fMLP are discussed in view of future drug development.