175530-90-2Relevant articles and documents
Synthesis of chiral benzimidazole-pyrrolidine derivatives and their application in organocatalytic aldol and Michael addition reactions
Reddy, K. Rajender,Krishna, G. Gopi,Rajasekhar
, p. 4289 - 4299 (2007)
An efficient and mild approach for the synthesis of pyrrolidine- benzimidazoles has been reported. They were further employed for the aldol and Michael addition reactions to afford the corresponding products with good yields and moderate enantioselectivit
Facile synthesis, characterization and antimicrobial activity of 2-alkanamino Benzimidazole derivatives
Ajani, Olayinka O.,Aderohunmu, Damilola V.,Olorunshola, Shade J.,Ikpo, Chinwe O.,Olanrewaju, Ifedolapo O.
, p. 109 - 120 (2016/05/09)
Benzimidazole derivatives are known to represent a class of medicinally important compounds which are extensively used in drug design and catalysis. A series of 2-substituted benzimidazole derivatives 10a-i was herein synthesized from the reaction of o-phenylenediamine with some amino acids using ameliorable pathway. The chemical structures of the synthesized compounds were confirmed by IR, UV, 1H-NMR, 13C-NMR, Mass spectral and analytical data. The compounds were investigated for their antimicrobial activity alongside gentamicin clinical standard. The results showed that this skeletal framework exhibited marked potency as antimicrobial agents. The most active compound was 1H-benzo[d]imidazol-2-yl)methanamine, 10a.
Peptide deformylase inhibitors of Mycobacterium tuberculosis: Synthesis, structural investigations, and biological results
Pichota, Arkadius,Duraiswamy, Jeyaraj,Yin, Zheng,Keller, Thomas H.,Alam, Jenefer,Liung, Sarah,Lee, Gladys,Ding, Mei,Wang, Gang,Chan, Wai Ling,Schreiber, Mark,Ma, Ida,Beer, David,Ngew, Xinyi,Mukherjee, Kakoli,Nanjundappa, Mahesh,Teo, Jeanette W.P.,Thayalan, Pamela,Yap, Amelia,Dick, Thomas,Meng, Wuyi,Xu, Mei,Koehn, James,Pan, Shi-Hao,Clark, Kirk,Xie, Xiaoling,Shoen, Carolyn,Cynamon, Michael
scheme or table, p. 6568 - 6572 (2009/09/30)
Bacterial peptide deformylase (PDF) belongs to a subfamily of metalloproteases catalyzing the removal of the N-terminal formyl group from newly synthesized proteins. We report the synthesis and biological activity of highly potent inhibitors of Mycobacterium tuberculosis (Mtb) PDF enzyme as well as the first X-ray crystal structure of Mtb PDF. Structure-activity relationship and crystallographic data clarified the structural requirements for high enzyme potency and cell based potency. Activities against single and multi-drug-resistant Mtb strains are also reported.