660451-26-3Relevant academic research and scientific papers
Design of potent dipeptidyl peptidase IV (DPP-4) inhibitors by employing a strategy to form a salt bridge with Lys554
Maezaki, Hironobu,Tawada, Michiko,Yamashita, Tohru,Banno, Yoshihiro,Miyamoto, Yasufumi,Yamamoto, Yoshio,Ikedo, Koji,Kosaka, Takuo,Tsubotani, Shigetoshi,Tani, Akiyoshi,Asakawa, Tomoko,Suzuki, Nobuhiro,Oi, Satoru
, p. 3565 - 3571 (2017)
We report a design strategy to obtain potent DPP-4 inhibitors by incorporating salt bridge formation with Lys554 in the S1′ pocket. By applying the strategy to the previously identified templates, quinoline 4 and pyridines 16a, 16b, and 17 have been identified as subnanomolar or nanomolar inhibitors of human DPP-4. Docking studies suggested that a hydrophobic interaction with Tyr547 as well as the salt bridge interaction is important for the extremely high potency. The design strategy would be useful to explore a novel design for DPP-4 inhibitors having a distinct structure with a unique binding mode.
FUSED HETEROCYCLIC COMPOUNDS
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Page 194-195, (2008/06/13)
A compound represented by the formula wherein ring A is an optionally substituted 5- to 10-membered aromatic ring; R1 and R2 are the same or different and each is an optionally substituted hydrocarbon group or an optionally substituted heterocyclic group; X and Y are the same or different and each is a bond, -O-, -S-, -SO-, -SO?2#191- or -NR3- (R3 is a hydrogen atom or an optionally substituted hydrocarbon group); and L is a divalent hydrocarbon group, or a salt thereof shows a superior peptidase-inhibitory activity and is useful as a prophylactic or therapeutic agent of diabetes and the like.
