KNI-10747 | 1300049-11-9

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 肽模拟物
• 英文名称: KNI-10747
• 英文别名: (4R)-N-(2,2-dimethylpropyl)-3-[(2S,3S)-2-hydroxy-3-[[(2S)-2-[[(2R)-2-hydroxy-2-phenylacetyl]amino]-3,3-dimethylbutanoyl]amino]-4-phenylbutanoyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxamide
• CAS: 1300049-11-9
• 化学式: C₃₅H₅₀N₄O₆S
• 分子量: 654.871
• InChiKey: UWTRJVWPXJVOPM-UZINISAASA-N

物化性质

• 沸点：
  940.5±65.0 °C(Predicted)
• 密度：
  1.189±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  4.8
• 重原子数：
  46
• 可旋转键数：
  13
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.54
• 拓扑面积：
  173
• 氢给体数：
  5
• 氢受体数：
  7

反应信息

• 作为产物：
  描述：

  特戊胺 在 盐酸 、 (benzotriazo-1-yloxy)tris(dimethylamino)phosphonium hexafluorophosphate 、 1-羟基苯并三唑 、 盐酸-N-乙基-Nˊ-(3-二甲氨基丙基)碳二亚胺 、 三乙胺 作用下， 以 1,4-二氧六环 、 N,N-二甲基甲酰胺 为溶剂， 反应 2.0h， 生成 KNI-10747
  参考文献：
  名称：

  Maintaining potent HTLV-I protease inhibition without the P3-cap moiety in small tetrapeptidic inhibitors

  摘要：

  The human T cell lymphotropic/leukemia virus type 1 (HTLV-I) causes adult T cell lymphoma/leukemia. The virus is also responsible for chronic progressive myelopathy and several inflammatory diseases. To stop the manufacturing of new viral components, in our previous reports, we derived small tetrapeptidic HTLV-I protease inhibitors with an important amide-capping moiety at the P-3 residue. In the current study, we removed the P-3-cap moiety and, with great difficulty, optimized the P-3 residue for HTLV-I protease inhibition potency. We discovered a very potent and small tetrapeptidic HTLV-I protease inhibitor (KNI-10774a, IC50 = 13 nM). (C) 2011 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2011.01.048

文献信息

• Maintaining potent HTLV-I protease inhibition without the P3-cap moiety in small tetrapeptidic inhibitors
  作者：Jeffrey-Tri Nguyen、Keiko Kato、Henri-Obadja Kumada、Koushi Hidaka、Tooru Kimura、Yoshiaki Kiso

  DOI：10.1016/j.bmcl.2011.01.048

  日期：2011.3

  The human T cell lymphotropic/leukemia virus type 1 (HTLV-I) causes adult T cell lymphoma/leukemia. The virus is also responsible for chronic progressive myelopathy and several inflammatory diseases. To stop the manufacturing of new viral components, in our previous reports, we derived small tetrapeptidic HTLV-I protease inhibitors with an important amide-capping moiety at the P-3 residue. In the current study, we removed the P-3-cap moiety and, with great difficulty, optimized the P-3 residue for HTLV-I protease inhibition potency. We discovered a very potent and small tetrapeptidic HTLV-I protease inhibitor (KNI-10774a, IC50 = 13 nM). (C) 2011 Elsevier Ltd. All rights reserved.