Phosphatidyl ethanolamine-binding proteins (PEBPs) are implicated in various critical physiological processes in all eukaryotes. Among them is Flowering Locus T (FT), the protein recently discovered as the vital flowering hormone in plants. Small molecule inhibitors and activators of FT could provide control over plant flowering and are therefore an interesting target for industrial agriculture. No small molecule inhibitors or activators are known for FT, but for a structurally similar PEBP, RKIP, an inhibitor called locostatin has been reported to covalently bind in the RKIP ligand binding pocket. Herein, we report the synthesis of novel locostatin-based chemical PEBP probes and evaluate their ability and selectivity towards the binding of FT and RKIP.