2,2,2-trifluoro-N-(2-(naphthalen-1-ylamino)ethyl)acetamide | 895775-85-6

• 分子结构分类: 有机化合物 - 苯类化合物 - 萘
• 英文名称: 2,2,2-trifluoro-N-(2-(naphthalen-1-ylamino)ethyl)acetamide
• 英文别名: 2,2,2-trifluoro-N-[2-(naphthalen-1-ylamino)ethyl]acetamide
• CAS: 895775-85-6
• 化学式: C₁₄H₁₃F₃N₂O
• 分子量: 282.265
• InChiKey: WWCWZLAFQNSCJW-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.6
• 重原子数：
  20
• 可旋转键数：
  4
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.21
• 拓扑面积：
  41.1
• 氢给体数：
  2
• 氢受体数：
  5

反应信息

• 作为产物：
  描述：

  三氟乙酸乙酯 、 N-(1-naphthyl)ethylenediamine dihydrochloride 在 水 、 N,N-二异丙基乙胺 作用下， 以 乙腈 为溶剂， 以86%的产率得到2,2,2-trifluoro-N-(2-(naphthalen-1-ylamino)ethyl)acetamide
  参考文献：
  名称：

  Polyamines Inhibit Carbonic Anhydrases by Anchoring to the Zinc-Coordinated Water Molecule

  摘要：

  Carbonic anhydrases (CAs, EC 4.2.1.1) are inhibited by sulfonamides, phenols, and coumarins. Polyamines such as spermine, spermidine, and many synthetic congeners are described to constitute a novel class of CA inhibitors (CAIs), interacting with the different CA isozymes with efficiency from the low nanomolar to millimolar range. The main structure activity relationship for these CAIs have been delineated: the length of the molecule, number of amine moieties, and their functionalization are the main parameters controlling activity. The X-ray crystal structure of the CA II spermine adduct allowed understanding of the inhibition mechanism. Spermine anchors to the nonprotein zinc ligand through a network of hydrogen bonds. Its distal amine moiety makes hydrogen bonds with residues Thr200 and Pro201, which further stabilize the adduct. Spermine binds differently compared to sulfonamides, phenols, or coumarins, rendering possible to develop CAIs with a diverse inhibition mechanism, profile, and selectivity for various isoforms.

  DOI：

  10.1021/jm1003667

文献信息

• Polyamines Inhibit Carbonic Anhydrases by Anchoring to the Zinc-Coordinated Water Molecule
  作者：Fabrizio Carta、Claudia Temperini、Alessio Innocenti、Andrea Scozzafava、Kai Kaila、Claudiu T. Supuran

  DOI：10.1021/jm1003667

  日期：2010.8.12

  Carbonic anhydrases (CAs, EC 4.2.1.1) are inhibited by sulfonamides, phenols, and coumarins. Polyamines such as spermine, spermidine, and many synthetic congeners are described to constitute a novel class of CA inhibitors (CAIs), interacting with the different CA isozymes with efficiency from the low nanomolar to millimolar range. The main structure activity relationship for these CAIs have been delineated: the length of the molecule, number of amine moieties, and their functionalization are the main parameters controlling activity. The X-ray crystal structure of the CA II spermine adduct allowed understanding of the inhibition mechanism. Spermine anchors to the nonprotein zinc ligand through a network of hydrogen bonds. Its distal amine moiety makes hydrogen bonds with residues Thr200 and Pro201, which further stabilize the adduct. Spermine binds differently compared to sulfonamides, phenols, or coumarins, rendering possible to develop CAIs with a diverse inhibition mechanism, profile, and selectivity for various isoforms.