566155-75-7Relevant articles and documents
Acridine-based agents with topoisomerase II activity inhibit pancreatic cancer cell proliferation and induce apoptosis
Goodell, John R.,Ougolkov, Andrei V.,Hiasa, Hiroshi,Kaur, Harneet,Remmel, Rory,Billadeau, Daniel D.,Ferguson, David M.
, p. 179 - 182 (2008)
A series of substituted 9-aminoacridines is evaluated for antiproliferative activity toward pancreatic cancer cells. The results indicate that the compounds inhibit cell proliferation by inducing a G1-S phase arrest. A model is also developed that explain
Compound a preparation UNC1215 method
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Paragraph 0036, (2017/03/14)
The invention discloses a method for preparing a compound UNC1215, belonging to the technical field of pharmaceutical chemistry synthesis. The method sequentially comprises the following steps: nitration, nitro reduction reaction, Buchwald reaction, esterolysis reaction, condensation reaction and the like. The overall reaction yield can reach 67%, which is higher than the yield (60%) in the document. The method changes the synthesis route, avoids the pipe sealing reaction, sequentially performs the nitration, reduction reaction, Buchwald reaction, hydrolysis reaction and condensation reaction, and is simple to operate.
Small-molecule ligands of methyl-lysine binding proteins: Optimization of selectivity for L3MBTL3
James, Lindsey I.,Korboukh, Victoria K.,Krichevsky, Liubov,Baughman, Brandi M.,Herold, J. Martin,Norris, Jacqueline L.,Jin, Jian,Kireev, Dmitri B.,Janzen, William P.,Arrowsmith, Cheryl H.,Frye, Stephen V.
, p. 7358 - 7371 (2013/10/21)
Lysine methylation is a key epigenetic mark, the dysregulation of which is linked to many diseases. Small-molecule antagonism of methyl-lysine (Kme) binding proteins that recognize such epigenetic marks can improve our understanding of these regulatory mechanisms and potentially validate Kme binding proteins as drug-discovery targets. We previously reported the discovery of 1 (UNC1215), the first potent and selective small-molecule chemical probe of a methyl-lysine reader protein, L3MBTL3, which antagonizes the mono- and dimethyl-lysine reading function of L3MBTL3. The design, synthesis, and structure-activity relationship studies that led to the discovery of 1 are described herein. These efforts established the requirements for potent L3MBTL3 binding and enabled the design of novel antagonists, such as compound 2 (UNC1679), that maintain in vitro and cellular potency with improved selectivity against other MBT-containing proteins. The antagonists described were also found to effectively interact with unlabeled endogenous L3MBTL3 in cells.
