A long-lived peptide-conjugated iridium(III)complex as a luminescent probe and inhibitorof the cell migration mediator, formyl peptidereceptor 2

摘要

Formyl peptide receptors play important biological and therapeutic roles in wound repair and inflammatorydiseases. In this work, we present a luminescent iridium(III) complex (6) conjugated with the peptide agonistWKYMVm as a luminescent formyl peptide receptor 2 (FPR2) imaging probe in living cells. Complex 6displayed ideal cell imaging characteristics, high photostability and low cytotoxicity. Competition assayswith a known FPR2 antagonist, WRW4, and siRNA knockdown experiments both revealed that complex 6selectively targeted FPR2 in living HUVEC cells. Moreover, complex 6 regulated FPR2 signalling in HUVECcells as shown using a mechanical scratch assay. Finally, complex 6 reduced epithelial cell migrationcapacity and inhibited lipoxin A4 (LXA4)-triggered cell migration in HUVEC cells, demonstrating theability of this complex to inhibit FPR2 in living cells. To our knowledge, this is the first long-lived probefor imaging FPR2 in living cells.