N⁴-(cinnamylidene)sulfanilamide | 59547-64-7

• 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: N⁴-(cinnamylidene)sulfanilamide
• 英文别名: N-cinnamylidene-sulfanilic acid amide；N-Cinnamyliden-sulfanilsaeure-amid；N-trans-Cinnamyliden-sulfanilsaeure-amid
• CAS: 59547-64-7
• 化学式: C₁₅H₁₄N₂O₂S
• 分子量: 286.354
• InChiKey: ABNOYMJFPBRWMR-FZHIPVGDSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.75
• 重原子数：
  20.0
• 可旋转键数：
  4.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  72.52
• 氢给体数：
  1.0
• 氢受体数：
  3.0

反应信息

• 作为产物：
  描述：

  磺胺 、 肉桂醛 以 甲醇 为溶剂， 以50%的产率得到N⁴-(cinnamylidene)sulfanilamide
  参考文献：
  名称：

  Carbonic anhydrase inhibitors. Part 43. Schiff bases derived from aromatic sulfonamides: towards more specific inhibitors for membrane-bound versus cytosolic isozymes

  摘要：

  Schiff bases were prepared by reaction of sulfanilamide, homosulfanilamide and p-aminoethyl-benzenesulfonamide with substituted benzene- and heterocyclic aldehydes. The compounds were characterized by standard procedures and were assayed as inhibitors of three isozymes of carbonic anhydrase (CA). Several of these new compounds showed a modest two-fold selectivity for the membrane-bound (bovine) isozyme, CA IV (bCA IV) as compared to the cytosolic human isozymes hCA I and II, in contrast to classical inhibitors which are 17-33 times less effective against bCA IV. This greater selectivity toward bCA IV is due mainly to a decreased potency against HCA II relative to classical inhibitors. This type of compound might lead to the development of low molecular weight isozyme specific CA IV inhibitors.

  DOI：

  10.1016/s0223-5234(97)81681-9

文献信息

• Carbonic anhydrase inhibitors. Part 43. Schiff bases derived from aromatic sulfonamides: towards more specific inhibitors for membrane-bound versus cytosolic isozymes
  作者：CT Supuran、A Scozzafava、A Popescu、R Bobes-Tureac、A Banciu、A Creanga、G Bobes-Tureac、MD Banciu

  DOI：10.1016/s0223-5234(97)81681-9

  日期：1997.5

  Schiff bases were prepared by reaction of sulfanilamide, homosulfanilamide and p-aminoethyl-benzenesulfonamide with substituted benzene- and heterocyclic aldehydes. The compounds were characterized by standard procedures and were assayed as inhibitors of three isozymes of carbonic anhydrase (CA). Several of these new compounds showed a modest two-fold selectivity for the membrane-bound (bovine) isozyme, CA IV (bCA IV) as compared to the cytosolic human isozymes hCA I and II, in contrast to classical inhibitors which are 17-33 times less effective against bCA IV. This greater selectivity toward bCA IV is due mainly to a decreased potency against HCA II relative to classical inhibitors. This type of compound might lead to the development of low molecular weight isozyme specific CA IV inhibitors.