Novel SAR for quinazoline inhibitors of EHMT1 and EHMT2

Autor:	Christoph Schächtele, Jan E. Ehlert, Ruben Gerardus George Leenders, Daniel Müller, Daniel Feger, Danny C. Lenstra, Jasmin Mecinović, Federica Trivarelli, Remco Zijlmans, Gerhard Müller, Bart van Bree, Anita Wegert, Marc van de Sande, Eddy Damen, Carolin Heidemann-Dinger, Michael H.G. Kubbutat
Rok vydání:	2019
Předmět:	Stereochemistry Clinical Biochemistry Lysine Pharmaceutical Science Synthetic Organic Chemistry 01 natural sciences Biochemistry Histones EHMT2 Inhibitory Concentration 50 Structure-Activity Relationship chemistry.chemical_compound Cell Line Tumor Histocompatibility Antigens Drug Discovery Quinazoline Humans Point Mutation Structure–activity relationship Enzyme Inhibitors Molecular Biology Binding Sites 010405 organic chemistry Organic Chemistry Substitution (logic) Histone-Lysine N-Methyltransferase 0104 chemical sciences Molecular Docking Simulation Pancreatic Neoplasms 010404 medicinal & biomolecular chemistry chemistry Drug Design Quinazolines Molecular Medicine Linker
Zdroj:	Bioorganic & Medicinal Chemistry Letters, 29, 2516-2524 Bioorganic & Medicinal Chemistry Letters, 29, 17, pp. 2516-2524
ISSN:	0960-894X
Popis:	Detailed structure activity relationship of two series of quinazoline EHMT1/EHMT2 inhibitors (UNC0224 and UNC0638) have been elaborated. New and active alternatives are presented for the ubiquitous substitution patterns found in literature for the linker to the lysine mimicking region and the lysine mimic itself. These findings could allow for advancing EHMT1/EHMT2 inhibitors of that type beyond tool compounds by fine-tuning physicochemical properties making these inhibitors more drug-like. .
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::371bee28b62d7f328781fc0bfa1f7d42 https://doi.org/10.1016/j.bmcl.2019.06.012 Zobrazit plný text záznamu Full Text from ScienceDirect