(R,Z)-2-(5-(4-(methoxycarbonyl)benzylidene)-4-oxo-2-thioxothiazolidin-3-yl)-3-phenylpropanoic acid | 1609466-52-5

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: (R,Z)-2-(5-(4-(methoxycarbonyl)benzylidene)-4-oxo-2-thioxothiazolidin-3-yl)-3-phenylpropanoic acid
• 英文别名: (2R)-2-[(5Z)-5-[(4-methoxycarbonylphenyl)methylidene]-4-oxo-2-sulfanylidene-1,3-thiazolidin-3-yl]-3-phenylpropanoic acid
• CAS: 1609466-52-5
• 化学式: C₂₁H₁₇NO₅S₂
• 分子量: 427.502
• InChiKey: BHZADHAJUMKNKJ-WISAJEAXSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.4
• 重原子数：
  29
• 可旋转键数：
  7
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.14
• 拓扑面积：
  141
• 氢给体数：
  1
• 氢受体数：
  7

反应信息

• 作为产物：
  描述：

  D-苯丙氨酸 在 溶剂黄146 、 sodium hydroxide 、 β-丙氨酸 作用下， 以 水 为溶剂， 反应 12.0h， 生成 (R,Z)-2-(5-(4-(methoxycarbonyl)benzylidene)-4-oxo-2-thioxothiazolidin-3-yl)-3-phenylpropanoic acid
  参考文献：
  名称：

  Discovery of the first potent and selective Mycobacterium tuberculosis Zmp1 inhibitor

  摘要：

  The Mycobacterium tuberculosis extracellular zinc metalloprotease 1 (Zmp1) has been proposed to play a key role in phagosome maturation and to enhance the survival of Mycobacterium tuberculosis in the host. Consequently, small molecule inhibitors of Zmp1 are of pivotal importance as a tool to better understand the pathogenicity of Zmp1 and as lead candidates for pharmacological intervention. Here we combined in silico structure-based inhibitor design with biochemical studies to discover and characterize the first potent competitive Zmp1 inhibitor showing a K-i of 94 nM and a high selectivity for Zmp1 with respect to human Neprilysin. (C) 2014 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2014.04.004

文献信息

• Discovery of the first potent and selective Mycobacterium tuberculosis Zmp1 inhibitor
  作者：Mattia Mori、Francesca Moraca、Davide Deodato、Davide M. Ferraris、Petra Selchow、Peter Sander、Menico Rizzi、Maurizio Botta

  DOI：10.1016/j.bmcl.2014.04.004

  日期：2014.6

  The Mycobacterium tuberculosis extracellular zinc metalloprotease 1 (Zmp1) has been proposed to play a key role in phagosome maturation and to enhance the survival of Mycobacterium tuberculosis in the host. Consequently, small molecule inhibitors of Zmp1 are of pivotal importance as a tool to better understand the pathogenicity of Zmp1 and as lead candidates for pharmacological intervention. Here we combined in silico structure-based inhibitor design with biochemical studies to discover and characterize the first potent competitive Zmp1 inhibitor showing a K-i of 94 nM and a high selectivity for Zmp1 with respect to human Neprilysin. (C) 2014 Elsevier Ltd. All rights reserved.