84445-93-2Relevant academic research and scientific papers
Identification of ortho-hydroxy anilide as a novel scaffold for lysine demethylase 5 inhibitors
Jaikhan, Pattaporn,Buranrat, Benjaporn,Itoh, Yukihiro,Chotitumnavee, Jiranan,Kurohara, Takashi,Suzuki, Takayoshi
supporting information, p. 1173 - 1176 (2019/03/29)
Fe(II)/α-ketoglutarate-dependent lysine demethylases (KDMs) are attractive drug targets for several diseases including cancer. In this study, we designed and screened ortho-substituted anilides that are expected to function as Fe(II) chelators, and identified ortho-hydroxy anilide as a novel scaffold for KDM5A inhibitors. Treatment of human lung cancer A549 cells with a prodrug form of 4-carboxy-2-hydroxy-formanilide (9c) increased trimethylated lysine 4 on histone H3 level, suggesting KDM5 inhibition in the cells.
Structure-Based Inhibitors of Influenza Virus Salidase. A Benzoic Acid Lead with Novel Interaction
Singh, Sangetta,Jedrzejas, Marek J.,Air, Gillian M.,Luo, Ming,Laver, W. Graeme,Brouillette, Wayne
, p. 3217 - 3225 (2007/10/03)
Influenza virus sialidase is a surface enzyme that is essential for infection of the virus.The catalytic site is highly conserved among all known influenza variants, suggesting that this protein is a suitable target for drug intervention.The most potent known inhibitors are analogs of 2-deoxy-2,3-didehydro-N-acetylneuraminic acid (Neu5Ac2en), particulary the 4-guanidino derivative (4-guanidino-Neu5Ac2en).We utilized the benzene ring of 4-(N-acetylamino)benzoic acids as a cyclic template to substitute for the dihydropyran ring of Neu5Ac2en.In this study several 3-(N-acylamino) derivatives were prepared as potential replacements for the glycerol side chain of Neu5Ac2en, and some were found to interact with the same binding subsite of sialidase.Of greater significance was the observation that the 3-guanidinobenzoic acid derivative (equivalent to the 4-guanidino grouping of 4-guanidino-Neu5Ac2en), the most potent benzoic acid inhibitor of influenza sialidase thus far identified (IC50 = 10 μM), occupied the glycerol-binding subsite on sialidase as opposed to the guanidino-binding subsite.This benzoic acid derivative thus provides a new compound that interacts in a novel manner with the catalytic site of influenza sialidase.
Synthesis of N-Acetylbenzimidazole Derivatives
Tanaka, Kenjiro,Shimazaki, Michiko,Murakami, Yasuoki
, p. 2714 - 2722 (2007/10/02)
For the structure determination of thiazolobenzimidazol-3(2H)-one derivatives (2 or 3) they were converted to the corresponding 1-acetylbenzimidazoles (4) by desulfurization.The latter compounds (4) were alternatively prepared by the cyclization of 2-aminoacetanilide derivatives (5) with CS2 in dimethylformamide (DMF), followed by desulfurization with Raney Ni.However, the reactions of 5 with ethyl orthoformate/H2SO4 in DMF gave a mixture of 4 and its acetyl-rearranged product (7).Keywords-acetyl group; rearrangement; thiazolobenzimidazol-3(2H)-one; N-acetylbenzimidazoles; ethyl orthoformate; carbon disulfide; desulfurization
