2-benzyl-4-fluoro-4-pentenoic acid | 205373-54-2

• 分子结构分类: 有机化合物 - 苯丙烷和聚酮 - 苯丙酸
• 英文名称: 2-benzyl-4-fluoro-4-pentenoic acid
• 英文别名: 2-Benzyl-4-fluoropent-4-enoic acid
• CAS: 205373-54-2
• 化学式: C₁₂H₁₃FO₂
• 分子量: 208.232
• InChiKey: BJDPTELPJLGYCH-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.7
• 重原子数：
  15
• 可旋转键数：
  5
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.25
• 拓扑面积：
  37.3
• 氢给体数：
  1
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  2-benzyl-4-fluoro-4-pentenoic acid 在 phosphate buffer 、 α-chimotripsine 、 乙酰氯 作用下， 以 水 为溶剂， 反应 14.0h， 生成 (R)-2-benzyl-4-fluoro-4-pentenoic acid
  参考文献：
  名称：

  A novel type of structurally simple nonpeptide inhibitors for α-chymotrypsin. Induced-fit binding of methyl 2-allyl-3-benzene-propanoate to the S2 subsite pocket

  摘要：

  Unexpectedly, methyl and benzyl esters of 2-allyl-3-benzenepropanoic acid were found to be not substrates but potent competitive inhibitors for alpha-chymotrypsin. The inhibitory property of the structurally simple nonpeptidic compounds is ascribed to their high binding affinity to the enzyme at the S-2 rather than S-1 subsite pocket. These inhibitors exist in a flexible form in solution, but as they bind to the enzyme bulky contrained conformers present in a minute concentration play an important role, forming tighter enzyme-inhibitor complexes by binding to the large hydrophobic S-2 pocket. The contrained conformers are thought to be resulted from intramolecular CH/pi interactions between a vinylic proton and the aromatic pi-electron cloud in the inhibitor molecules. These compounds constitute novel examples of the induced-fit binding inhibitor of possibly simplest structure. (C) 1998 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0968-0896(97)10038-4
• 作为产物：
  描述：

  2-benzyl-4-pentenoic acid 在 吡啶 、 N-溴代丁二酰亚胺(NBS) 、 lithium aluminium tetrahydride 、 jones' reagent 、 potassium tert-butylate 、 二异丁基氢化铝 、 氟化氢吡啶 、 乙酰氯 作用下， 以 四氢呋喃 、 二氯甲烷 、 丙酮 为溶剂， 反应 33.5h， 生成 2-benzyl-4-fluoro-4-pentenoic acid
  参考文献：
  名称：

  A novel type of structurally simple nonpeptide inhibitors for α-chymotrypsin. Induced-fit binding of methyl 2-allyl-3-benzene-propanoate to the S2 subsite pocket

  摘要：

  Unexpectedly, methyl and benzyl esters of 2-allyl-3-benzenepropanoic acid were found to be not substrates but potent competitive inhibitors for alpha-chymotrypsin. The inhibitory property of the structurally simple nonpeptidic compounds is ascribed to their high binding affinity to the enzyme at the S-2 rather than S-1 subsite pocket. These inhibitors exist in a flexible form in solution, but as they bind to the enzyme bulky contrained conformers present in a minute concentration play an important role, forming tighter enzyme-inhibitor complexes by binding to the large hydrophobic S-2 pocket. The contrained conformers are thought to be resulted from intramolecular CH/pi interactions between a vinylic proton and the aromatic pi-electron cloud in the inhibitor molecules. These compounds constitute novel examples of the induced-fit binding inhibitor of possibly simplest structure. (C) 1998 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0968-0896(97)10038-4