7-(morpholinomethyl)-5-nitroquinolin-8-ol | 74440-53-2

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 喹啉及其衍生物
• 英文名称: 7-(morpholinomethyl)-5-nitroquinolin-8-ol
• 英文别名: 7-morpholinomethyl-5-nitro-quinolin-8-ol；7-Morpholinomethyl-5-nitro-chinolin-8-ol；7-(Morpholinomethyl)-5-nitro-8-hydroxyquinoline；8-Quinolinol, 7-(4-morpholinylmethyl)-5-nitro-；7-(morpholin-4-ylmethyl)-5-nitroquinolin-8-ol
• CAS: 74440-53-2
• 化学式: C₁₄H₁₅N₃O₄
• 分子量: 289.291
• InChiKey: JGPOSHZTEOQDBZ-UHFFFAOYSA-N

物化性质

• 熔点：
  213-215 °C
• 沸点：
  506.1±50.0 °C(Predicted)
• 密度：
  1.414±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  1.1
• 重原子数：
  21
• 可旋转键数：
  2
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.36
• 拓扑面积：
  91.4
• 氢给体数：
  1
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  乙二醇乙醚 、 7-(morpholinomethyl)-5-nitroquinolin-8-ol 生成 7-morpholinomethyl-quinoline-5,8-dione
  参考文献：
  名称：

  一些喹啉5：8醌

  摘要：

  DOI：

  10.1039/jr9540000570
• 作为产物：
  描述：

  5-亚硝基-8-羟基喹啉 在 硝酸 作用下， 以 乙醇 、 水 为溶剂， 反应 25.25h， 生成 7-(morpholinomethyl)-5-nitroquinolin-8-ol
  参考文献：
  名称：

  8-羟基喹啉衍生物的合成和抗植物病原体活性†

  摘要：

  植物病原真菌已成为全球农产品质量、粮食安全和人类健康的严重威胁，需要发现具有从头化学支架和高效的新型抗真菌剂。设计并合成了一系列8-羟基喹啉衍生物，并评估了它们对五种植物病原真菌的抗真菌活性。体外试验表明，大多数受试化合物对五种目标真菌有显着影响，其抑制活性优于阳性对照嘧菌酯。特别是化合物2，在所有测试的化合物中表现出最高的效力，EC 50分别为 0.0021、0.0016、0.0124、0.0059 和 0.0120 mM 对灰霉病菌、核盘菌、禾谷镰刀菌、尖孢镰刀菌和米分枝杆菌，然后是化合物5c。光学显微镜和扫描电镜的形态观察表明，化合物2和5c引起核盘菌菌丝异常。此外，化合物2和5c对核盘菌的体内抗真菌活性结果表明，5c具有比2更强的保护和治疗活性，40和80 μg mL -1 5c的疗效（84.18%和95.44%）优于嘧菌酯（77.32%和83.59%）。因此，化合物2和5c有望成为开发新型杀菌剂的新型先导结构。

  DOI：

  10.1039/c9ra05712a

文献信息

• Organoruthenated Nitroxoline Derivatives Impair Tumor Cell Invasion through Inhibition of Cathepsin B Activity
  作者：Ana Mitrović、Jakob Kljun、Izidor Sosič、Matija Uršič、Anton Meden、Stanislav Gobec、Janko Kos、Iztok Turel

  DOI：10.1021/acs.inorgchem.9b01882

  日期：2019.9.16

  cysteine peptidase cathepsin B (catB) is an important tumor-promoting factor involved in tumor progression and metastasis representing a relevant target for the development of new antitumor agents. In the present study, we synthesized 11 ruthenium compounds bearing either the clinical agent nitroxoline that was previously identified as potent selective reversible inhibitor of catB activity or its derivatives

  溶酶体半胱氨酸肽酶组织蛋白酶B（catB）是重要的肿瘤促进因子，参与肿瘤的进展和转移，是开发新型抗肿瘤药物的相关靶标。在本研究中，我们合成了11种钌化合物，它们带有先前被鉴定为catB活性的强效选择性可逆抑制剂或其衍生物的临床药物硝氧嘧啶。我们证明有机钌化是一种获得catB内肽和外肽酶活性的高效和特异性抑制剂的可行策略，如使用酶动力学和微尺度热泳所显示的。此外，我们显示了在低非细胞毒性浓度下，基于catB抑制作用的新型金属药物在体外基于细胞的功能测定中显着损害了肿瘤进展的过程。一般来说，
• 8-hydroxyquinolines as inhibitors of cathepsin B
  申请人：University of Ljubljana

  公开号：EP2353599A1

  公开（公告）日：2011-08-10

  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.

  本发明涉及化合物或其药用可接受的盐、水合物或溶剂化物，这些化合物是半胱氨酸蛋白酶抑制剂，特别是猫hepsin B的抑制剂。本发明的化合物在治疗与猫hepsin B有关的疾病中有用，例如癌症、类风湿性关节炎、骨关节炎、骨质疏松症、胰腺炎、免疫和神经退行性疾病，例如阿尔茨海默病。
• Discovery of Inhibitors of <i>Burkholderia pseudomallei</i> Methionine Aminopeptidase with Antibacterial Activity
  作者：Phumvadee Wangtrakuldee、Matthew S. Byrd、Cristine G. Campos、Michael W. Henderson、Zheng Zhang、Michael Clare、Ali Masoudi、Peter J. Myler、James R. Horn、Peggy A. Cotter、Timothy J. Hagen

  DOI：10.1021/ml400034m

  日期：2013.8.8

  Evaluation of a series of MetAP inhibitors in an in vitro enzyme activity assay led to the first identification of potent molecules that show significant growth inhibition against Burkholderia pseudomallei. Nitroxoline analogues show excellent inhibition potency in the BpMetAP1 enzyme activity assay with the lowest IC50 of 30 nM and inhibit the growth of B. pseudomallei and B. thailandensis at concentrations >= 31 mu M.
• Rickettsia prowazekii methionine aminopeptidase as a promising target for the development of antibacterial agents
  作者：Travis R. Helgren、Congling Chen、Phumvadee Wangtrakuldee、Thomas E. Edwards、Bart L. Staker、Jan Abendroth、Banumathi Sankaran、Nicole A. Housley、Peter J. Myler、Jonathon P. Audia、James R. Horn、Timothy J. Hagen

  DOI：10.1016/j.bmc.2016.11.013

  日期：2017.2

  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. (C) 2016 Elsevier Ltd. All rights reserved.
• Movrin; Maysinger; Marok, Pharmazie, 1980, vol. 35, # 8, p. 458 - 460
  作者：Movrin、Maysinger、Marok

  DOI：——

  日期：——