[(S)-1-((S)-1-Benzyl-2-hydroxy-2-phenethylcarbamoyl-ethylcarbamoyl)-3-methyl-butyl]-carbamic acid benzyl ester | 316830-82-7

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 肽模拟物
• 英文名称: [(S)-1-((S)-1-Benzyl-2-hydroxy-2-phenethylcarbamoyl-ethylcarbamoyl)-3-methyl-butyl]-carbamic acid benzyl ester
• CAS: 316830-82-7
• 化学式: C₃₂H₃₉N₃O₅
• 分子量: 545.679
• InChiKey: JTXCWDGLUFUPRO-ASYYUYISSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.77
• 重原子数：
  40.0
• 可旋转键数：
  14.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.34
• 拓扑面积：
  116.76
• 氢给体数：
  4.0
• 氢受体数：
  5.0

反应信息

• 作为反应物：
  描述：

  [(S)-1-((S)-1-Benzyl-2-hydroxy-2-phenethylcarbamoyl-ethylcarbamoyl)-3-methyl-butyl]-carbamic acid benzyl ester 在 戴斯-马丁氧化剂 作用下， 生成 [(S)-1-((S)-1-Benzyl-2-oxo-2-phenethylcarbamoyl-ethylcarbamoyl)-3-methyl-butyl]-carbamic acid benzyl ester
  参考文献：
  名称：

  Synthesis and calpain inhibitory activity of α-ketoamides with 2,3-methanoleucine stereoisomers at the P2 position

  摘要：

  A series of novel ketoamides incorporating all four 2,3-methanoleucine stereoisomers at the P-2 position was synthesized. The compounds displayed a wide variation in K-i values for inhibition of calpain I depending on the configuration of the P-2 methanoleucine residue. However, similar variation in cathepsin B inhibition was not observed suggesting that the S-2 pocket of calpain I is more stereosensitive than that of cathepsin B. (C) 2000 Published by Elsevier Science Ltd.

  DOI：

  10.1016/s0960-894x(00)00518-7
• 作为产物：
  描述：

  tert-butyl ((2S)-1-cyano-1-hydroxy-3-phenylpropan-2-yl)carbamate 在 盐酸 、 sodium hydroxide 、 1-羟基苯并三唑 、 1-(3-二甲基氨基丙基)-3-乙基碳二亚胺 作用下， 以 1,4-二氧六环 为溶剂， 生成 [(S)-1-((S)-1-Benzyl-2-hydroxy-2-phenethylcarbamoyl-ethylcarbamoyl)-3-methyl-butyl]-carbamic acid benzyl ester
  参考文献：
  名称：

  Synthesis and calpain inhibitory activity of α-ketoamides with 2,3-methanoleucine stereoisomers at the P2 position

  摘要：

  A series of novel ketoamides incorporating all four 2,3-methanoleucine stereoisomers at the P-2 position was synthesized. The compounds displayed a wide variation in K-i values for inhibition of calpain I depending on the configuration of the P-2 methanoleucine residue. However, similar variation in cathepsin B inhibition was not observed suggesting that the S-2 pocket of calpain I is more stereosensitive than that of cathepsin B. (C) 2000 Published by Elsevier Science Ltd.

  DOI：

  10.1016/s0960-894x(00)00518-7

文献信息

• Significance of Hydrogen Bonding at the S1′ Subsite of Calpain I
  作者：Isaac O. Donkor、Xiaozhang Zheng、Jie Han、Calvin Lacy、Duane D. Miller

  DOI：10.1016/s0960-894x(01)00301-8

  日期：2001.7

  alpha -Ketohydroxamates were synthesized as bioisosteres of alpha -ketoamides. The alpha -ketohydroxamates were generally more potent than the corresponding alpha -ketoamides. The potency of the compounds suggests that hydrogen bonding and steric bulk of substituents on the nitrogen atom of the ketoamide moiety influence calpain inhibition. (C) 2001 Elsevier Science Ltd. All rights reserved.