2-benzyl-valeric acid methyl ester

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 脂肪酰基
• 英文名称: 2-benzyl-valeric acid methyl ester
• 英文别名: 2-Benzyl-valeriansaeure-methylester；Methyl 2-benzylpentanoate
• 化学式: C₁₃H₁₈O₂
• 分子量: 206.285
• InChiKey: VHQOJNHESYEDEC-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.5
• 重原子数：
  15
• 可旋转键数：
  6
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.46
• 拓扑面积：
  26.3
• 氢给体数：
  0
• 氢受体数：
  2

反应信息

• 作为产物：
  描述：

  methyl 2-benzylpent-4-enoate 在 palladium on activated charcoal 氢气 作用下， 以 甲醇 为溶剂， 反应 3.0h， 以96%的产率得到2-benzyl-valeric acid methyl ester
  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

文献信息

• Ketene Acetals. XVII. The Alkylation and Acylation of Substituted Ketene Acetals
  作者：S. M. McElvain、R. E. Kent、Calvin L. Stevens

  DOI：10.1021/ja01214a015

  日期：1946.10
• 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
  作者：Dong H. Kim、Zhi-Hong Li、Soo Suk Lee、Jeong-il Park、Sang J. Chung

  DOI：10.1016/s0968-0896(97)10038-4

  日期：1998.2

  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.