N-hexylbenzimidazole-1-carboxamide | 93605-65-3

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 苯并咪唑类
• 英文名称: N-hexylbenzimidazole-1-carboxamide
• 英文别名: Benzoimidazole-1-carboxylic acid hexylamide
• CAS: 93605-65-3
• 化学式: C₁₄H₁₉N₃O
• 分子量: 245.324
• InChiKey: NBEXETZHMIKKJK-UHFFFAOYSA-N

物化性质

• 密度：
  1.12±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  3.5
• 重原子数：
  18
• 可旋转键数：
  5
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.43
• 拓扑面积：
  46.9
• 氢给体数：
  1
• 氢受体数：
  2

反应信息

• 作为产物：
  描述：

  苯并咪唑 、 异氰酸己酯 以 乙醚 为溶剂， 反应 3.0h， 以79%的产率得到N-hexylbenzimidazole-1-carboxamide
  参考文献：
  名称：

  氨基酸衍生的潜在异氰酸酯：猪胰弹性蛋白酶和人白细胞弹性蛋白酶的不可逆失活。

  摘要：

  已经合成了几种氨基酸衍生的偶氮内酯（I），并研究了它们对人白细胞弹性蛋白酶和猪胰弹性蛋白酶的抑制活性。发现抑制活性取决于前体氨基酸酯的性质。因此，发现衍生自L-缬氨酸甲酯3，L-正缬氨酸甲酯5，DL-正亮氨酸甲酯9和L-甲硫氨酸甲酯10的化合物不可逆地抑制两种酶。发现化合物10是人白细胞弹性蛋白酶的特异性和选择性抑制剂。与这些相反，发现衍生自甘氨酸甲酯1，D-缬氨酸甲酯4和D-去甲缬氨酸甲酯6的抑制剂是无活性的。

  DOI：

  10.1021/jm00380a010

文献信息

• Amino acid derived latent isocyanates: irreversible inactivation of porcine pancreatic elastase and human leukocyte elastase
  作者：William C. Groutas、William R. Abrams、Michael C. Theodorakis、Annette M. Kasper、Steven A. Rude、Robert C. Badger、Timothy D. Ocain、Kevin E. Miller、Min K. Moi

  DOI：10.1021/jm00380a010

  日期：1985.2

  were found to inhibit irreversibly both enzymes. Compound 10 was found to be a specific and selective inhibitor of human leukocyte elastase. In contrast to these, inhibitors derived from glycine methyl ester 1, D-valine methyl ester 4, and D-norvaline methyl ester 6 were found to be inactive. The results of the present study show that latent isocyanates derived from appropriate amino acids can serve as

  已经合成了几种氨基酸衍生的偶氮内酯（I），并研究了它们对人白细胞弹性蛋白酶和猪胰弹性蛋白酶的抑制活性。发现抑制活性取决于前体氨基酸酯的性质。因此，发现衍生自L-缬氨酸甲酯3，L-正缬氨酸甲酯5，DL-正亮氨酸甲酯9和L-甲硫氨酸甲酯10的化合物不可逆地抑制两种酶。发现化合物10是人白细胞弹性蛋白酶的特异性和选择性抑制剂。与这些相反，发现衍生自甘氨酸甲酯1，D-缬氨酸甲酯4和D-去甲缬氨酸甲酯6的抑制剂是无活性的。
• Pharmacophore Identification and Scaffold Exploration to Discover Novel, Potent, and Chemically Stable Inhibitors of Acid Ceramidase in Melanoma Cells
  作者：Jose Antonio Ortega、Jose M. Arencibia、Giuseppina La Sala、Marco Borgogno、Inga Bauer、Luca Bono、Clarissa Braccia、Andrea Armirotti、Stefania Girotto、Anand Ganesan、Marco De Vivo

  DOI：10.1021/acs.jmedchem.7b00472

  日期：2017.7.13

  Acid ceramidase (AC) hydrolyzes ceramides, which are central lipid messengers for metabolism and signaling of sphingolipids. A growing body of evidence links deregulation of sphingolipids to several diseases, including cancer. Indeed, AC expression is abnormally high in melanoma cells. AC inhibition may thus be key to treating malignant melanoma. Here, we have used a systematic scaffold exploration to design a general pharmacophore for AC inhibition. This pharmacophore comprises a 6 + 5 fused ring heterocycle linked to an aliphatic substituent via a urea moiety. We have thus identified the novel benzimidazole derivatives 10, 21, 27, and 30, which are highly potent AC inhibitors. Their chemical and metabolic stabilities are comparable or superior to those of previously reported AC inhibitors. Moreover, they are potent against endogenous AC in intact melanoma cells. These novel inhibitors merit further characterization and can serve as a promising starting point for the discovery of new antimelanoma therapeutics.