S-[2-(2-ethylanilino)-2-oxoethyl] N-[[(2S)-3-[(4-methoxyphenyl)methoxy]-2-methylpropanoyl]amino]carbamothioate | 1250915-80-0

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: S-[2-(2-ethylanilino)-2-oxoethyl] N-[[(2S)-3-[(4-methoxyphenyl)methoxy]-2-methylpropanoyl]amino]carbamothioate
• CAS: 1250915-80-0
• 化学式: C₂₃H₂₉N₃O₅S
• 分子量: 459.566
• InChiKey: KBXZIALMFBSIFQ-INIZCTEOSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.5
• 重原子数：
  32
• 可旋转键数：
  11
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.35
• 拓扑面积：
  131
• 氢给体数：
  3
• 氢受体数：
  6

反应信息

• 作为产物：
  描述：

  S-[2-(2-ethylanilino)-2-oxoethyl] N-[[(2S)-3-hydroxy-2-methylpropanoyl]amino]carbamothioate 、 2-(4-甲氧基苄氧基)-3-硝基吡啶 在 CSA 作用下， 以 二氯甲烷 为溶剂， 反应 3.0h， 以16%的产率得到S-[2-(2-ethylanilino)-2-oxoethyl] N-[[(2S)-3-[(4-methoxyphenyl)methoxy]-2-methylpropanoyl]amino]carbamothioate
  参考文献：
  名称：

  Design, Synthesis and Biological Evaluation of a Library of Thiocarbazates and Their Activity as Cysteine Protease Inhibitors

  摘要：

  最近，我们鉴定出一类新型高效组织蛋白酶L抑制剂，其特点是具有硫卡巴脒头部结构。鉴于这些化合物有可能抑制其他半胱氨酸蛋白酶，我们设计并合成了一系列硫卡巴脒类化合物，这些化合物在三个位点上含有多样性元素。该化合物的生物活性鉴定结果显示，它们对木瓜蛋白酶家族的半胱氨酸蛋白酶相较于丝氨酸、金属蛋白酶以及某些类别的半胱氨酸蛋白酶（如胱天蛋白酶）表现出显著的选择性。我们鉴定出了几个高效的组织蛋白酶L和S抑制剂。通过对接研究，我们利用SAR数据来理解实现组织蛋白酶S抑制所需的结构要素。这项研究为设计高度有效且选择性的木瓜蛋白酶家族半胱氨酸蛋白酶抑制剂奠定了基础。

  DOI：

  10.2174/138620710791054303

文献信息

• Inhibitors of Human Cathepsin L, Cathepsin B, and Cathepsin S
  申请人：Diamond Scott L.

  公开号：US20110207726A1

  公开（公告）日：2011-08-25

  The present invention is directed to novel protease inhibitors that are specific for cathepsin L, cathepsin B, and cathepsin S. Accordingly, the present invention encompasses compositions and methods for treating and preventing diseases and disorders associated with cathepsin L, cathepsin B, or cathepsin S function or activity.
• [EN] INHIBITORS OF HUMAN CATHEPSIN L, CATHEPSIN B, AND CATHEPSIN S<br/>[FR] INHIBITEURS DES CATHEPSINES L, B ET S HUMAINES
  申请人：UNIV PENNSYLVANIA

  公开号：WO2009136997A2

  公开（公告）日：2009-11-12

  The present invention is directed to novel protease inhibitors that are specific for cathepsin L, cathepsin B, and cathepsin S. Accordingly, the present invention encompasses compositions and methods for treating and preventing diseases and disorders associated with cathepsin L, cathepsin B, or cathepsin S function or activity.
• Design, Synthesis and Biological Evaluation of a Library of Thiocarbazates and Their Activity as Cysteine Protease Inhibitors
  作者：Zhuqing Liu、Michael C. Myers、Parag P. Shah、Mary Pat Beavers、Phillip A. Benedetti、Scott L. Diamond、Amos B. Smith,III、Donna M. Huryn

  DOI：10.2174/138620710791054303

  日期：2010.5.1

  Recently, we identified a novel class of potent cathepsin L inhibitors, characterized by a thiocarbazate warhead. Given the potential of these compounds to inhibit other cysteine proteases, we designed and synthesized a library of thiocarbazates containing diversity elements at three positions. Biological characterization of this library for activity against a panel of proteases indicated a significant preference for members of the papain family of cysteine proteases over serine, metallo-, and certain classes of cysteine proteases, such as caspases. Several potent inhibitors of cathepsin L and S were identified. The SAR data were employed in docking studies in an effort to understand the structural elements required for cathepsin S inhibition. This study provides the basis for the design of highly potent and selective inhibitors of the papain family of cysteine proteases.

  最近，我们鉴定出一类新型高效组织蛋白酶L抑制剂，其特点是具有硫卡巴脒头部结构。鉴于这些化合物有可能抑制其他半胱氨酸蛋白酶，我们设计并合成了一系列硫卡巴脒类化合物，这些化合物在三个位点上含有多样性元素。该化合物的生物活性鉴定结果显示，它们对木瓜蛋白酶家族的半胱氨酸蛋白酶相较于丝氨酸、金属蛋白酶以及某些类别的半胱氨酸蛋白酶（如胱天蛋白酶）表现出显著的选择性。我们鉴定出了几个高效的组织蛋白酶L和S抑制剂。通过对接研究，我们利用SAR数据来理解实现组织蛋白酶S抑制所需的结构要素。这项研究为设计高度有效且选择性的木瓜蛋白酶家族半胱氨酸蛋白酶抑制剂奠定了基础。