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. Author manuscript; available in PMC: 2010 Jun 1.
Published in final edited form as: Pharmacol Rev. 2009 Jun 4;61(2):119–161. doi: 10.1124/pr.109.001578

Figure 5. Chemical structures of selected ligands for the formyl peptide receptors.

Figure 5

Despite their abilities to bind to FPR1 and/or FPR2/ALX, these ligands have quite different structures. Of the ligands shown, t-Boc-FLFLF and cyclosporin H (CsH) are antagonists, and others are agonists. Note that the N-formyl group that defines agonistic activities in peptides such as fMLF is replaced with a bulky t-butyloxycarbonyl group that defines antagonistic activities in peptides such as t-Boc-FLFLF. LXA4, Quin-C1 and Compound 43 are highly selective agonists for FPR2/ALX, whereas AG-14 and fMLF are selective for FPR1. t-Boc-FLFLF is selective for FPR1 at low concentrations but the selectivity is lost at high micromolar concentrations (e.g. 100μM).