25115-74-6Relevant articles and documents
Antimalarial activity of 2,6-dibenzylidenecyclohexanone derivatives
Eagon, Scott,Hammill, Jared T.,Fitzsimmons, Kasey,Sienko, Natalie,Nguyen, Brandon,Law, Jarvis,Manjunath, Aashrita,Wilkinson, Steven P.,Thompson, Kara,Glidden, Julia Elizabeth,Rice, Amy L.,Falade, Mofolusho O.,Kimball, Joshua J.,DiBernardo, Celine,Guy, R. Kiplin
, (2021)
Malaria remains one of the deadliest infectious diseases worldwide and continues to infect hundreds of millions of individuals each year. Here we report the discovery and derivatization of a series of 2,6-dibenzylidenecyclohexanones targeting the chloroquine-sensitive 3D7 strain of Plasmodium falciparum. While the initial lead compound displayed significant toxicity in a human cell proliferation assay, we were able to identify a derivative with no detectable toxicity and sub-micromolar potency.
Discovery of C-(1-aryl-cyclohexyl)-methylamines as selective, orally available inhibitors of dipeptidyl peptidase IV
Namoto, Kenji,Sirockin, Finton,Ostermann, Nils,Gessier, Francois,Flohr, Stefanie,Sedrani, Richard,Gerhartz, Bernd,Trappe, J?rg,Hassiepen, Ulrich,Duttaroy, Alokesh,Ferreira, Suzie,Sutton, Jon M.,Clark, David E.,Fenton, Garry,Beswick, Mandy,Baeschlin, Daniel K.
, p. 731 - 736 (2014/02/14)
The successful launches of dipeptidyl peptidase IV (DPP IV) inhibitors as oral anti-diabetics warrant and spur the further quest for additional chemical entities in this promising class of therapeutics. Numerous pharmaceutical companies have pursued their proprietary candidates towards the clinic, resulting in a large body of published chemical structures associated with DPP IV. Herein, we report the discovery of a novel chemotype for DPP IV inhibition based on the C-(1-aryl-cyclohexyl)-methylamine scaffold and its optimization to compounds which selectively inhibit DPP IV at low-nM potency and exhibit an excellent oral pharmacokinetic profile in the rat. 2014 Elsevier Ltd. All rights reserved.
Optimization of novel di-substituted cyclohexylbenzamide derivatives as potent 11β-HSD1 inhibitors
McMinn, Dustin L.,Rew, Yosup,Sudom, Athena,Caille, Seb,DeGraffenreid, Michael,He, Xiao,Hungate, Randall,Jiang, Ben,Jaen, Juan,Julian, Lisa D.,Kaizerman, Jacob,Novak, Perry,Sun, Daqing,Tu, Hua,Ursu, Stefania,Walker, Nigel P.C.,Yan, Xuelei,Ye, Qiuping,Wang, Zhulun,Powers, Jay P.
scheme or table, p. 1446 - 1450 (2010/01/16)
Novel 4,4-disubstituted cyclohexylbenzamide inhibitors of 11β-HSD1 were optimized to account for liabilities relating to in vitro pharmacokinetics, cytotoxicity and protein-related shifts in potency. A representative compound showing favorable in vivo pharmacokinetics was found to be an efficacious inhibitor of 11β-HSD1 in a rat pharmacodynamic model (ED50 = 10 mg/kg).