WKYMVM is a potent N-formyl peptide receptor (FPR1) and FPRL1/2 agonist, also activates several leukocyte effector functions such as chemotaxis, mobilization of complement receptor-3, and activation of the NADPH oxidase.
CAT No: R1753
CAS No:187986-17-0
Synonyms/Alias:WKYMVm;187986-17-0;D-Methioninamide, L-tryptophyl-L-lysyl-L-tyrosyl-L-methionyl-L-valyl-;Trp-Lys-Tyr-Met-Val-D-Met-NH2;CHEMBL552527;(2S)-6-amino-2-[[(2S)-2-amino-3-(1H-indol-3-yl)propanoyl]amino]-N-[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2R)-1-amino-4-methylsulfanyl-1-oxobutan-2-yl]amino]-3-methyl-1-oxobutan-2-yl]amino]-4-methylsulfanyl-1-oxobutan-2-yl]amino]-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]hexanamide;Trp-Lys-Tyr-Met-Val-D-Met-NH(2);(S)-6-amino-2-((S)-2-amino-3-(1H-indol-3-yl)propanamido)-N-((5R,8S,11S,14S)-5-carbamoyl-15-(4-hydroxyphenyl)-8-isopropyl-11-(2-(methylthio)ethyl)-7,10,13-trioxo-2-thia-6,9,12-triazapentadecan-14-yl)hexanamide;W-K-Y-M-V-M-NH2;HY-P1120;BDBM50295513;AKOS024456791;DA-68709;MS-31584;CS-0027964;G13471;(2S)-6-amino-2-[(2S)-2-amino-3-(1H-indol-3-yl)propanamido]-N-[(1S)-1-{[(1S)-1-{[(1S)-1-{[(1R)-1-carbamoyl-3-(methylsulfanyl)propyl]carbamoyl}-2-methylpropyl]carbamoyl}-3-(methylsulfanyl)propyl]carbamoyl}-2-(4-hydroxyphenyl)ethyl]hexanamide;
WKYMVM is a synthetic hexapeptide known for its role as a potent agonist of the formyl peptide receptor 2 (FPR2), a member of the G protein-coupled receptor family involved in immune cell signaling. As a peptide compound, WKYMVM mimics natural chemotactic peptides and is widely recognized for its utility in dissecting the molecular mechanisms underlying leukocyte migration, inflammation, and host defense. Its structural design allows for high receptor selectivity and robust functional responses in cellular assays, making it a valuable tool for researchers investigating innate immunity, signal transduction, and receptor pharmacology.
Chemotaxis studies: WKYMVM is extensively utilized in research focused on immune cell chemotaxis, particularly the directed migration of neutrophils and monocytes. By selectively activating FPR2, it enables precise delineation of downstream signaling pathways that govern cellular movement in response to infection or tissue damage. Its application in in vitro chemotaxis assays helps elucidate the roles of specific peptide-receptor interactions in orchestrating immune surveillance and inflammatory responses.
Receptor pharmacology: The peptide serves as a reference agonist for characterizing FPR2-mediated signaling events. It provides a robust platform for screening novel receptor modulators, antagonists, or biased agonists, thereby advancing the understanding of receptor-ligand specificity and functional selectivity. Studies employing WKYMVM have contributed to mapping the structural determinants of FPR2 activation and the consequences of receptor engagement on intracellular signaling cascades such as calcium flux, MAPK activation, and chemokine production.
Inflammation research: WKYMVM is instrumental in exploring the cellular and molecular mechanisms of inflammation. By selectively triggering FPR2, it allows researchers to model acute and chronic inflammatory processes in vitro, facilitating investigations into the recruitment and activation of leukocytes, the release of pro-inflammatory mediators, and the resolution of inflammatory responses. Its use in these contexts supports the development of new hypotheses regarding the regulation of immune cell function and tissue homeostasis.
Signal transduction analysis: The peptide is frequently applied in studies dissecting intracellular signaling networks downstream of FPR2 activation. Its high potency and receptor selectivity enable clear attribution of observed effects to specific signaling pathways. Researchers leverage WKYMVM to probe G protein coupling, second messenger generation, and the activation of effector proteins, providing insights into the integration of external signals that drive immune cell behavior.
Peptide-receptor interaction studies: WKYMVM's defined sequence and receptor specificity make it an excellent probe for structural and biophysical investigations of peptide-receptor interactions. It is used in binding assays, mutagenesis studies, and computational modeling to understand the molecular basis of FPR2 recognition and activation. Such research informs the rational design of novel peptide ligands and therapeutic candidates targeting the formyl peptide receptor family, broadening the scope of peptide-based research in immunology and pharmacology.
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