1,4-Dithia-spiro[4.5]decane-6-carboxylic acid | 337468-24-3

• 分子结构分类: 有机化合物 - 有机硫化合物 - 硫代缩醛
• 英文名称: 1,4-Dithia-spiro[4.5]decane-6-carboxylic acid
• 英文别名: 1,4-Dithiaspiro[4.5]decane-6-carboxylic acid
• CAS: 337468-24-3
• 化学式: C₉H₁₄O₂S₂
• 分子量: 218.341
• InChiKey: CIXCOSSSJHLKQB-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.2
• 重原子数：
  13
• 可旋转键数：
  1
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.89
• 拓扑面积：
  87.9
• 氢给体数：
  1
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  1,4-Dithia-spiro[4.5]decane-6-carboxylic acid 在 二苯基磷酸 、 N,N-二异丙基乙胺 作用下， 以 苯 为溶剂， 生成 1,4-Dithia-spiro[4.5]decane-6-carbonyl azide
  参考文献：
  名称：

  Using the Electrostatic Field Effect to Design a New Class of Inhibitors for Cysteine Proteases

  摘要：

  A new class of competitive inhibitors for the cysteine protease papain is described. These inhibitors are based upon a 4-heterocyclohexanone ring and are designed to react with the enzyme active site nucleophile to give a reversibly formed hemithioketal. The electrophilicity of the ketone in these inhibitors is enhanced by ring strain and by through-space electrostatic repulsion with the heteroatom at the 1-position of the ring. Equilibrium constants for addition of water and 3-mercaptopropionic acid to several 4-heterocyclohexanones were measured by H-1 NMR spectroscopy. These reactions model addition of the active site nucleophile to the corresponding inhibitors. The equilibrium constants give a linear correlation with the field substituent constant F for the functional group at the 1-position of the heterocyclohexanone. These equilibrium constants also correlate well with the inhibition constants for the 4-heterocyclohexanone-based inhibitors, which range from 11 to 120 mu M. Thus, the model system can be used to predict the potency of structurally related enzyme inhibitors.

  DOI：

  10.1021/ja9641867
• 作为产物：
  描述：

  2-环己酮甲酸乙酯 在 sodium hydroxide 、 对甲苯磺酸 作用下， 以 甲醇 为溶剂， 生成 1,4-Dithia-spiro[4.5]decane-6-carboxylic acid
  参考文献：
  名称：

  Using the Electrostatic Field Effect to Design a New Class of Inhibitors for Cysteine Proteases

  摘要：

  A new class of competitive inhibitors for the cysteine protease papain is described. These inhibitors are based upon a 4-heterocyclohexanone ring and are designed to react with the enzyme active site nucleophile to give a reversibly formed hemithioketal. The electrophilicity of the ketone in these inhibitors is enhanced by ring strain and by through-space electrostatic repulsion with the heteroatom at the 1-position of the ring. Equilibrium constants for addition of water and 3-mercaptopropionic acid to several 4-heterocyclohexanones were measured by H-1 NMR spectroscopy. These reactions model addition of the active site nucleophile to the corresponding inhibitors. The equilibrium constants give a linear correlation with the field substituent constant F for the functional group at the 1-position of the heterocyclohexanone. These equilibrium constants also correlate well with the inhibition constants for the 4-heterocyclohexanone-based inhibitors, which range from 11 to 120 mu M. Thus, the model system can be used to predict the potency of structurally related enzyme inhibitors.

  DOI：

  10.1021/ja9641867

文献信息

• Using the Electrostatic Field Effect to Design a New Class of Inhibitors for Cysteine Proteases
  作者：Jeffrey L. Conroy、Tanya C. Sanders、Christopher T. Seto

  DOI：10.1021/ja9641867

  日期：1997.5.1

  A new class of competitive inhibitors for the cysteine protease papain is described. These inhibitors are based upon a 4-heterocyclohexanone ring and are designed to react with the enzyme active site nucleophile to give a reversibly formed hemithioketal. The electrophilicity of the ketone in these inhibitors is enhanced by ring strain and by through-space electrostatic repulsion with the heteroatom at the 1-position of the ring. Equilibrium constants for addition of water and 3-mercaptopropionic acid to several 4-heterocyclohexanones were measured by H-1 NMR spectroscopy. These reactions model addition of the active site nucleophile to the corresponding inhibitors. The equilibrium constants give a linear correlation with the field substituent constant F for the functional group at the 1-position of the heterocyclohexanone. These equilibrium constants also correlate well with the inhibition constants for the 4-heterocyclohexanone-based inhibitors, which range from 11 to 120 mu M. Thus, the model system can be used to predict the potency of structurally related enzyme inhibitors.