In vitro characterization of luseogliflozin,a potent and competitive sodium glucose co-transporter 2 inhibitor: Inhibition kinetics and binding studies

In this study,we evaluated an inhibition model of luseogliflozin on sodium glucose co-transporter 2 (sglt2). we also analyzed the binding kinetics of the drug to sglt2 protein using [3h]-luseogliflozin. luseogliflozin competitively inhibited human sglt2 (hsglt2)-mediated glucose uptake with a ki value of 1.10 nm. in the absence of glucose,[3h]-luseogliflozin exhibited a high affinity for hsglt2 with a kd value of 1.3 nm. the dissociation half-time was 7 h,suggesting that luseogliflozin dissociates rather slowly from hsglt2. these profiles of luseogliflozin might contribute to the long duration of action of this drug. © 2015 taisho pharmaceutical co.,ltd. ltd. production and hosting by elsevier b.v. on behalf of japanese pharmacological society. this is an open access article under the cc by-nc-nd license.