N-(furan-2-ylmethyl)-3-oxobenzo[d]isothiazole-2(3H)-carboxamide | 1601403-03-5

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 苯并噻唑类
• 英文名称: N-(furan-2-ylmethyl)-3-oxobenzo[d]isothiazole-2(3H)-carboxamide
• 英文别名: N-(furan-2-ylmethyl)-3-oxobenzo[d]isothiazole-2(3H)-carboxamide；N-(furan-2-ylmethyl)-3-oxo-1,2-benzothiazole-2-carboxamide
• CAS: 1601403-03-5
• 化学式: C₁₃H₁₀N₂O₃S
• 分子量: 274.3
• InChiKey: IRBBDJYBNHNLKO-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.2
• 重原子数：
  19
• 可旋转键数：
  2
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.08
• 拓扑面积：
  87.8
• 氢给体数：
  1
• 氢受体数：
  4

反应信息

• 作为产物：
  描述：

  1,2-苯并异噻唑-3-酮 在 4-二甲氨基吡啶 、 三乙胺 作用下， 以 四氢呋喃 、 二氯甲烷 为溶剂， 反应 0.5h， 生成 N-(furan-2-ylmethyl)-3-oxobenzo[d]isothiazole-2(3H)-carboxamide
  参考文献：
  名称：

  1,2-Benzisothiazol-3-one derivatives as a novel class of small-molecule caspase-3 inhibitors

  摘要：

  A novel series of 1,2-benzisothiazol-3-one derivatives was synthesized and their biological activities were evaluated for inhibiting caspase-3 and -7 activities, in which some of them showed low nanomolar potency against caspase-3 in vitro and significant protection against apoptosis in a camptothecin-induced Jurkat T cells system. Among the tested compounds, compound 5i exhibited the most potent caspase-3 inhibitory activity (IC50 = 1.15 nM). The molecular docking predicted the interactions and binding modes of the synthesized inhibitor in the caspase-3 active site. (C) 2014 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2014.03.002

文献信息

• Ebsulfur as a potent scaffold for inhibition and labelling of New Delhi metallo-β-lactamase-1 in vitro and in vivo
  作者：Jianpeng Su、Jiayun Liu、Cheng Chen、Yuejuan Zhang、Kewu Yang

  DOI：10.1016/j.bioorg.2018.11.035

  日期：2019.3

  The superbug infection caused by New Delhi metallo-beta-lactamase (NDM-1) has grown into an emerging threat, labelling and inhibition of NDM-1 has proven challenging due to its shuttling between pathogenic bacteria. Here, we report a potent covalent scaffold, ebsulfur, for targeting the protein in vitro and in vivo. Enzymatic kinetic study indicated that eighteen ebsulfurs gained except 1a-b and 1f inhibited NDM-1, exhibiting an IC50 value ranging of 0.16-9 mu M, and 1g was found to be the best, dose- and time-dependent inhibitor with an IC50 of 0.16 mu M. Also, these ebsulfurs effectively restored the antibacterial activity of cefazolin against E. coli expressing NDM-1, and the best effect was observed to be from 1g, 1i and 1n, resulting in an 256-fold reduction in MIC of the antibiotic at a dose of 16 mu g/mL. The equilibrium dialysis study implied that the ebsulfur disrupted the coordination of one Zn(II) ion at active site of NDM-1. Labelling of NDM-1 using a constructed fluorescent ebsulfur Ebs-R suggested that the inhibitor covalently bound to the target through SDS-PAGE analysis in vitro. Also, labelling NDM-1 in living E. coli cells with Ebs-R by confocal microscopic imaging showed the real-time distribution change process of intracellular recombinant protein NDM-1. Moreover, the cytotoxicity of these ebsulfurs against L929 mouse fibroblastic cells was tested, and their capability to restore antibacterial activity of antibiotic against clinical strains E. coli ECO8 producing NDM-1 was determined. The ebsulfur scaffold proposed here is valuable for development of the covalent irreversible inhibitors of NDM-1, and also for labelling the target in vitro and in vivo.
• 1,2-Benzisothiazol-3-one derivatives as a novel class of small-molecule caspase-3 inhibitors
  作者：Lixin Wu、Meiqi Lu、Zhihui Yan、Xiaobin Tang、Bo Sun、Wei Liu、Honggang Zhou、Cheng Yang

  DOI：10.1016/j.bmc.2014.03.002

  日期：2014.4

  A novel series of 1,2-benzisothiazol-3-one derivatives was synthesized and their biological activities were evaluated for inhibiting caspase-3 and -7 activities, in which some of them showed low nanomolar potency against caspase-3 in vitro and significant protection against apoptosis in a camptothecin-induced Jurkat T cells system. Among the tested compounds, compound 5i exhibited the most potent caspase-3 inhibitory activity (IC50 = 1.15 nM). The molecular docking predicted the interactions and binding modes of the synthesized inhibitor in the caspase-3 active site. (C) 2014 Elsevier Ltd. All rights reserved.