Screening of protonstatin-1 (PS-1) analogs for improved inhibitors of plant plasma membrane H+-ATPase activity

We previously identified protonstatin-1 (PS-1) as a selective inhibitor of plasma membrane H⁺-ATPase (PM H⁺-ATPase) activity and used it as a tool to validate the chemiosmotic model for polar Auxin transport. Here, to obtain compounds with higher affinity than PS-1 for PM H⁺-ATPase, we synthesized 34 PS-1 analogs and examined their ability to inhibit PM H⁺-ATPase activity. The 34 analogs showed varying inhibitory effects on the activity of this Enzyme. The strongest effect was observed for the small molecule PS-2, which was approximately five times stronger than PS-1. Compared to PS-1, PS-2 was also a stronger inhibitor of Auxin uptake as well as acropetal and basipetal polar Auxin transport in Arabidopsis thaliana seedlings. Because PS-2 is a more potent inhibitor of PM H⁺-ATPase than PS-1, we believe that this compound could be used as a tool to study the functions of this key plant Enzyme.

PS-2; arabidopsis; auxin transport; inhibitor; plasma membrane H+-ATPase.