(R)-2-(4-Methoxy-benzenesulfonylamino)-succinic acid 1-methyl ester | 350697-33-5

• 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)-2-(4-Methoxy-benzenesulfonylamino)-succinic acid 1-methyl ester
• CAS: 350697-33-5
• 化学式: C₁₂H₁₅NO₇S
• 分子量: 317.32
• InChiKey: RQVWFALOPWCBDM-SNVBAGLBSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.01
• 重原子数：
  21.0
• 可旋转键数：
  7.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.33
• 拓扑面积：
  119.0
• 氢给体数：
  2.0
• 氢受体数：
  6.0

反应信息

• 作为反应物：
  描述：

  (R)-2-(4-Methoxy-benzenesulfonylamino)-succinic acid 1-methyl ester 在 1-羟基苯并三唑 、 盐酸-N-乙基-Nˊ-(3-二甲氨基丙基)碳二亚胺 、 三苯基膦 、 偶氮二甲酸二乙酯 作用下， 以 二氯甲烷 、 N,N-二甲基甲酰胺 为溶剂， 生成 (3R,9aS)-2-(4-Methoxy-benzenesulfonyl)-5-oxo-octahydro-pyrrolo[1,2-a][1,4]diazepine-3-carboxylic acid methyl ester
  参考文献：
  名称：

  Heterocycle-based MMP Inhibitors with P2′ Substituents

  摘要：

  Potent and selective inhibition of matrix metalloproteinases was demonstrated fur a series of sulfonamide-based hydroxamic acids. The design of the heterocyclic sulfonamides incorporates a six- or seven-member central ring with a P2 ' substituent that can be modified. Binding interactions of this substituent at the S2 ' site are believed to contribute to high inhibitory potency against stromelysin, collagenase-3 and gelatinases A and B, and to provide selectivity against collagenase-1 and matrilysin. An X-ray structure of a stromelysin-inhibitor complex was obtained to provide insights into the SAR and selectivity trends observed for the series. (C) 2001 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0960-894x(01)00137-8
• 作为产物：
  描述：

  (R)-2-(4-Methoxy-benzenesulfonylamino)-succinic acid 4-tert-butyl ester 1-methyl ester 在 三氟乙酸 作用下， 以 二氯甲烷 为溶剂， 生成 (R)-2-(4-Methoxy-benzenesulfonylamino)-succinic acid 1-methyl ester
  参考文献：
  名称：

  Heterocycle-based MMP Inhibitors with P2′ Substituents

  摘要：

  Potent and selective inhibition of matrix metalloproteinases was demonstrated fur a series of sulfonamide-based hydroxamic acids. The design of the heterocyclic sulfonamides incorporates a six- or seven-member central ring with a P2 ' substituent that can be modified. Binding interactions of this substituent at the S2 ' site are believed to contribute to high inhibitory potency against stromelysin, collagenase-3 and gelatinases A and B, and to provide selectivity against collagenase-1 and matrilysin. An X-ray structure of a stromelysin-inhibitor complex was obtained to provide insights into the SAR and selectivity trends observed for the series. (C) 2001 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0960-894x(01)00137-8