219509-79-2Relevant articles and documents
Site-Selective C-H Alkylation of Piperazine Substrates via Organic Photoredox Catalysis
McManus, Joshua B.,Onuska, Nicholas P. R.,Jeffreys, Matthew S.,Goodwin, Nicole C.,Nicewicz, David A.
, p. 679 - 683 (2020)
Piperazine-containing compounds serve as one of the most important classes of compounds throughout all fields of chemistry. Alas, current synthetic methods have fallen short of providing a general method for the synthesis of highly decorated piperazine fragments. Herein, we present a site-selective approach to the C-H functionalization of existing piperazine compounds using photoredox catalysis. This manifold relies on the predictable differentiation of electronically distinct nitrogen centers within the piperazine framework, granting access to novel C-alkylated variants of the starting piperazines.
Substituted phenoxypropyl-(R)-2-methylpyrrolidine aminomethyl ketones as histamine-3 receptor inverse agonists
Zulli, Allison L.,Aimone, Lisa D.,Mathiasen, Joanne R.,Gruner, John A.,Raddatz, Rita,Bacon, Edward R.,Hudkins, Robert L.
scheme or table, p. 2807 - 2810 (2012/05/20)
Optimization of a series of aminomethyl ketone diamine H3R antagonists to reduce the brain exposure by lowering the pKa, led to molecules with improved pharmacokinetic properties. Compounds 9, 19, and 25 had high affinity for human H3R and demonstrated in vivo H3R functional activity in the rat dipsogenia model. Compound 9 displayed modest wake-promoting activity in the rat EEG/EMG model.
Synthesis and SAR of 4-carboxy-2-azetidinone mechanism-based tryptase inhibitors
Sutton, James C.,Bolton, Scott A.,Hartl, Karen S.,Huang, Ming-Hsing,Jacobs, Glenn,Meng, Wei,Ogletree, Martin L.,Pi, Zulan,Schumacher, William A.,Seiler, Steven M.,Slusarchyk, William A.,Treuner, Uwe,Zahler, Robert,Zhao, Guohua,Bisacchi, Gregory S.
, p. 3229 - 3233 (2007/10/03)
A series of N1-activated C4-carboxy azetidinones was prepared and tested as inhibitors of human tryptase. The key stereochemical and functional features required for potency, serine protease specificity and aqueous stability were determined. From these studies compound 2, BMS-262084, was identified as a potent and selective tryptase inhibitor which, when dosed intratracheally in ovalbumin-sensitized guinea pigs, reduced allergen-induced bronchoconstriction and inflammatory cell infiltration into the lung.