MMV675997 | 1224923-38-9

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 二嗪烷类
• 英文名称: MMV675997
• 英文别名: Benzyl cyanomethyl(4-(4-(4-fluorophenyl)piperazin-1-yl)butyl)carbamate；benzyl N-(cyanomethyl)-N-[4-[4-(4-fluorophenyl)piperazin-1-yl]butyl]carbamate
• CAS: 1224923-38-9
• 化学式: C₂₄H₂₉FN₄O₂
• 分子量: 424.518
• InChiKey: UQOCJNOTNWYZQR-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.9
• 重原子数：
  31
• 可旋转键数：
  10
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.42
• 拓扑面积：
  59.8
• 氢给体数：
  0
• 氢受体数：
  6

反应信息

• 作为产物：
  描述：

  、 1-(4-氟苯基)哌嗪 以 二氯甲烷 为溶剂， 以17%的产率得到MMV675997
  参考文献：
  名称：

  Design and evaluation of Trypanosoma brucei metacaspase inhibitors

  摘要：

  Metacaspase (MCA) is an important enzyme in Trypanosoma brucei, absent from humans and differing significantly from the orthologous human caspases. Therefore MCA constitutes a new attractive drug target for antiparasitic chemotherapeutics, which needs further characterization to support the discovery of innovative drug candidates. A first series of inhibitors has been prepared on the basis of known substrate specificity and the predicted catalytic mechanism of the enzyme. In this Letter we present the first inhibitors of TbMCA2 with low micromolar enzymatic and antiparasitic activity in vitro combined with low cytotoxicity. (C) 2010 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2010.01.099

文献信息

• Design and evaluation of Trypanosoma brucei metacaspase inhibitors
  作者：Maya Berg、Pieter Van der Veken、Jurgen Joossens、Venkatraj Muthusamy、Matthias Breugelmans、Catherine X. Moss、Jana Rudolf、Paul Cos、Graham H. Coombs、Louis Maes、Achiel Haemers、Jeremy C. Mottram、Koen Augustyns

  DOI：10.1016/j.bmcl.2010.01.099

  日期：2010.3

  Metacaspase (MCA) is an important enzyme in Trypanosoma brucei, absent from humans and differing significantly from the orthologous human caspases. Therefore MCA constitutes a new attractive drug target for antiparasitic chemotherapeutics, which needs further characterization to support the discovery of innovative drug candidates. A first series of inhibitors has been prepared on the basis of known substrate specificity and the predicted catalytic mechanism of the enzyme. In this Letter we present the first inhibitors of TbMCA2 with low micromolar enzymatic and antiparasitic activity in vitro combined with low cytotoxicity. (C) 2010 Elsevier Ltd. All rights reserved.