Yoshida_2012_Bioorg.Med.Chem_20_5033

Reference

Title : Fused bicyclic heteroarylpiperazine-substituted L-prolylthiazolidines as highly potent DPP-4 inhibitors lacking the electrophilic nitrile group - Yoshida_2012_Bioorg.Med.Chem_20_5033
Author(s) : Yoshida T , Akahoshi F , Sakashita H , Sonda S , Takeuchi M , Tanaka Y , Nabeno M , Kishida H , Miyaguchi I , Hayashi Y
Ref : Bioorganic & Medicinal Chemistry , 20 :5033 , 2012
Abstract :

Hypoglycemic agents with a mechanism of depeptidyl peptidase IV (DPP-4) inhibition are suitable for once daily oral dosing. It is difficult to strike a balance between inhibitory activity and duration of action in plasma for inhibitors bearing an electrophilic nitrile group. We explored fused bicyclic heteroarylpiperazine substituted at the gamma-position of the proline structure in the investigation of L-prolylthiazolidines lacking the electrophilic nitrile. Among them, 2-trifluoroquinolyl compound 8g is the most potent, long-lasting DPP-4 inhibitor (IC(50) = 0.37 nmol/L) with high selectivity against other related peptidases. X-ray crystal structure determination of 8g indicates that CH-pi interactions generated between the quinolyl ring and the guanidinyl group of Arg358 enhances the DPP-4 inhibitory activity and selectivity.

PubMedSearch : Yoshida_2012_Bioorg.Med.Chem_20_5033
PubMedID: 22824762
Gene_locus related to this paper: human-DPP4

Related information

Inhibitor CHEMBL2147710    CHEMBL2058971
Gene_locus human-DPP4
Structure 3VJK    3VJL    3VJM

Citations formats

Yoshida T, Akahoshi F, Sakashita H, Sonda S, Takeuchi M, Tanaka Y, Nabeno M, Kishida H, Miyaguchi I, Hayashi Y (2012)
Fused bicyclic heteroarylpiperazine-substituted L-prolylthiazolidines as highly potent DPP-4 inhibitors lacking the electrophilic nitrile group
Bioorganic & Medicinal Chemistry 20 :5033

Yoshida T, Akahoshi F, Sakashita H, Sonda S, Takeuchi M, Tanaka Y, Nabeno M, Kishida H, Miyaguchi I, Hayashi Y (2012)
Bioorganic & Medicinal Chemistry 20 :5033