74440-53-2Relevant articles and documents
Synthesis and anti-phytopathogenic activity of 8-hydroxyquinoline derivatives
Yin, Xiao-Dan,Sun, Yu,Lawoe, Raymond Kobla,Yang, Guan-Zhou,Liu, Ying-Qian,Shang, Xiao-Fei,Liu, Hua,Yang, Yu-Dong,Zhu, Jia-Kai,Huang, Xiao-Ling
, p. 30087 - 30099 (2019/10/04)
Phytopathogenic fungi have become a serious threat to the quality of agricultural products, food security and human health globally, necessitating the need to discover new antifungal agents with de novo chemical scaffolds and high efficiency. A series of 8-hydroxyquinoline derivatives were designed and synthesized, and their antifungal activity was evaluated against five phytopathogenic fungi. In vitro assays revealed that most of the tested compounds remarkably impacted the five target fungi and their inhibitory activities were better than that of the positive control azoxystrobin. Compound 2, in particular, exhibited the highest potency among all the tested compounds, with an EC50 of 0.0021, 0.0016, 0.0124, 0.0059 and 0.0120 mM respectively against B. cinerea, S. sclerotiorum, F. graminearum, F. oxysporum and M. oryzae, followed by compound 5c. The morphological observations of optical microscopy and scanning electron microscopy revealed that compounds 2 and 5c caused mycelial abnormalities of S. sclerotiorum. Futhermore, the results of in vivo antifungal activity of compounds 2 and 5c against S. sclerotiorum showed that 5c possessed stronger protective and curative activity than that of 2, and the curative effects of 5c at 40 and 80 μg mL-1 (84.18% and 95.44%) were better than those of azoxystrobin (77.32% and 83.59%). Therefore, compounds 2 and 5c are expected to be novel lead structures for the development of new fungicides.
Rickettsia prowazekii methionine aminopeptidase as a promising target for the development of antibacterial agents
Helgren, Travis R.,Chen, Congling,Wangtrakuldee, Phumvadee,Edwards, Thomas E.,Staker, Bart L.,Abendroth, Jan,Sankaran, Banumathi,Housley, Nicole A.,Myler, Peter J.,Audia, Jonathon P.,Horn, James R.,Hagen, Timothy J.
supporting information, p. 813 - 824 (2017/02/05)
Methionine aminopeptidase (MetAP) is a class of ubiquitous enzymes essential for the survival of numerous bacterial species. These enzymes are responsible for the cleavage of N-terminal formyl-methionine initiators from nascent proteins to initiate post-translational modifications that are often essential to proper protein function. Thus, inhibition of MetAP activity has been implicated as a novel antibacterial target. We tested this idea in the present study by targeting the MetAP enzyme in the obligate intracellular pathogen Rickettsia prowazekii. We first identified potent RpMetAP inhibitory species by employing an in vitro enzymatic activity assay. The molecular docking program AutoDock was then utilized to compare published crystal structures of inhibited MetAP species to docked poses of RpMetAP. Based on these in silico and in vitro screens, a subset of 17 compounds was tested for inhibition of R. prowazekii growth in a pulmonary vascular endothelial cell (EC) culture infection model system. All compounds were tested over concentration ranges that were determined to be non-toxic to the ECs and 8 of the 17 compounds displayed substantial inhibition of R. prowazekii growth. These data highlight the therapeutic potential for inhibiting RpMetAP as a novel antimicrobial strategy and set the stage for future studies in pre-clinical animal models of infection.
8-hydroxyquinolines as inhibitors of cathepsin B
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, (2011/09/12)
This invention relates to the compounds or a pharmaceutical acceptable salts, hydrates or solvates thereof, which are inhibitors of cysteine proteases, in particular of cathepsin B. Compounds of the invention are useful in the treatment of diseases in which cathepsin B is implicated, such as cancer, rheumatoid arthritis, osteoarthritis, osteoporosis, pancreatitis, immune and neurodegenerative diseases, e.g. Alzheimer's disease.
