[4-(Thiiran-2-ylmethylsulfonyl)phenyl] propane-2-sulfonate | 1260222-35-2

• 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: [4-(Thiiran-2-ylmethylsulfonyl)phenyl] propane-2-sulfonate
• CAS: 1260222-35-2
• 化学式: C₁₂H₁₆O₅S₃
• 分子量: 336.454
• InChiKey: IYYMUUNQUMPQRB-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2
• 重原子数：
  20
• 可旋转键数：
  6
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.5
• 拓扑面积：
  120
• 氢给体数：
  0
• 氢受体数：
  6

反应信息

• 作为产物：
  描述：

  4-羟基苯硫酚 在 咪唑 、 potassium carbonate 、 三乙胺 、 N,N-二异丙基乙胺 、 硫脲 、 间氯过氧苯甲酸 作用下， 以 甲醇 、 二氯甲烷 、 N,N-二甲基甲酰胺 为溶剂， 反应 240.17h， 生成 [4-(Thiiran-2-ylmethylsulfonyl)phenyl] propane-2-sulfonate
  参考文献：
  名称：

  Sulfonate-Containing Thiiranes as Selective Gelatinase Inhibitors

  摘要：

  Matrix metalloproteinases (MMPs) are important zinc-dependent endopeptidases. Two members of this family of enzymes called gelatinases (MMP-2 and MMP-9) have been implicated in a number of human diseases, including cancer, neurological and cardiovascular diseases, and inflammation to name a few. We describe in this report the preparation and evaluation of two structural types of thiirane inhibitors that show selectivity toward gelatinases. The biphenyl series targets both gelatinases, whereas the monophenyl analogues exhibit potent inhibition of only MMP-2. The latter structural type also exhibits improved water solubility and metabolic stability, both traits desirable for progress of these molecules forward in gelatinase-dependent animal models of disease.

  DOI：

  10.1021/ml100254e

文献信息

• Sulfonate-Containing Thiiranes as Selective Gelatinase Inhibitors
  作者：Sebastian A. Testero、Mijoon Lee、Rachel T. Staran、Mana Espahbodi、Leticia I. Llarrull、Marta Toth、Shahriar Mobashery、Mayland Chang

  DOI：10.1021/ml100254e

  日期：2011.2.10

  Matrix metalloproteinases (MMPs) are important zinc-dependent endopeptidases. Two members of this family of enzymes called gelatinases (MMP-2 and MMP-9) have been implicated in a number of human diseases, including cancer, neurological and cardiovascular diseases, and inflammation to name a few. We describe in this report the preparation and evaluation of two structural types of thiirane inhibitors that show selectivity toward gelatinases. The biphenyl series targets both gelatinases, whereas the monophenyl analogues exhibit potent inhibition of only MMP-2. The latter structural type also exhibits improved water solubility and metabolic stability, both traits desirable for progress of these molecules forward in gelatinase-dependent animal models of disease.