(S)-4-{(S)-2-Benzyloxycarbonylamino-3-[4-(di-tert-butoxy-phosphoryloxy)-phenyl]-propionylamino}-4-dipentylcarbamoyl-butyric acid tert-butyl ester | 205236-45-9

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: (S)-4-{(S)-2-Benzyloxycarbonylamino-3-[4-(di-tert-butoxy-phosphoryloxy)-phenyl]-propionylamino}-4-dipentylcarbamoyl-butyric acid tert-butyl ester
• 英文别名: tert-butyl (4S)-4-[[(2S)-3-[4-[bis[(2-methylpropan-2-yl)oxy]phosphoryloxy]phenyl]-2-(phenylmethoxycarbonylamino)propanoyl]amino]-5-(dipentylamino)-5-oxopentanoate
• CAS: 205236-45-9
• 化学式: C₄₄H₇₀N₃O₁₀P
• 分子量: 832.028
• InChiKey: HRSPHCBSSKTIMA-BCRBLDSWSA-N

物化性质

• 沸点：
  860.896±65.00 °C(Press: 760.00 Torr)(predicted)
• 密度：
  1.110±0.06 g/cm3(Temp: 25 °C; Press: 760 Torr)(predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  8.5
• 重原子数：
  58
• 可旋转键数：
  28
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.64
• 拓扑面积：
  159
• 氢给体数：
  2
• 氢受体数：
  10

反应信息

• 作为反应物：
  描述：

  (S)-4-{(S)-2-Benzyloxycarbonylamino-3-[4-(di-tert-butoxy-phosphoryloxy)-phenyl]-propionylamino}-4-dipentylcarbamoyl-butyric acid tert-butyl ester 在 palladium on activated charcoal 氢气 、 1-羟基苯并三唑 、 三乙胺 、 N,N'-二环己基碳二亚胺 作用下， 以 甲醇 、 二氯甲烷 、 N,N-二甲基甲酰胺 为溶剂， 20.0 ℃ 、101.33 kPa 条件下， 反应 3.0h， 生成 (S)-4-{(S)-3-[4-(Di-tert-butoxy-phosphoryloxy)-phenyl]-2-phenylacetylamino-propionylamino}-4-dipentylcarbamoyl-butyric acid tert-butyl ester
  参考文献：
  名称：

  Potent Dipeptide Inhibitors of the pp60^c-src SH2 Domain

  摘要：

  The design, synthesis, and evaluation of dipeptide analogues as ligands for the pp60(c-src) SH2 domain are described. The critical binding interactions between Ac-Tyr-Glu-N(n-C5H11)(2) (2) and the protein are established and form the basis for our structure-based drug design efforts. The effects of changes in both the C-terminal (11-27) and N-terminal (51-69) portions of the dipeptide are explored. Analogues with reduced overall charge (92-95) are also investigated. We demonstrate the feasibility of pairing structurally diverse subunits in a modest dipeptide framework with the goal of increasing the druglike attributes without sacrificing binding affinity.

  DOI：

  10.1021/jm970853a
• 作为产物：
  描述：

  N-苄氧羰基-L-谷氨酸γ-叔丁酯 在 palladium on activated charcoal N-甲基吗啉 、 氢气 、 sodium hydride 、 1-羟基苯并三唑 、 三乙胺 、 N,N'-二环己基碳二亚胺 作用下， 以 四氢呋喃 、 甲醇 、 二氯甲烷 、 N,N-二甲基甲酰胺 为溶剂， -20.0~25.0 ℃ 、101.33 kPa 条件下， 反应 38.58h， 生成 (S)-4-{(S)-2-Benzyloxycarbonylamino-3-[4-(di-tert-butoxy-phosphoryloxy)-phenyl]-propionylamino}-4-dipentylcarbamoyl-butyric acid tert-butyl ester
  参考文献：
  名称：

  Potent Dipeptide Inhibitors of the pp60^c-src SH2 Domain

  摘要：

  The design, synthesis, and evaluation of dipeptide analogues as ligands for the pp60(c-src) SH2 domain are described. The critical binding interactions between Ac-Tyr-Glu-N(n-C5H11)(2) (2) and the protein are established and form the basis for our structure-based drug design efforts. The effects of changes in both the C-terminal (11-27) and N-terminal (51-69) portions of the dipeptide are explored. Analogues with reduced overall charge (92-95) are also investigated. We demonstrate the feasibility of pairing structurally diverse subunits in a modest dipeptide framework with the goal of increasing the druglike attributes without sacrificing binding affinity.

  DOI：

  10.1021/jm970853a

文献信息

• Potent Dipeptide Inhibitors of the pp60<i>^c</i><i>^-</i><i>^src</i> SH2 Domain
  作者：Gregory J. Pacofsky、Karen Lackey、Krystal J. Alligood、Judd Berman、Paul S. Charifson、Renae M. Crosby、George F. Dorsey,、Paul L. Feldman、Tona M. Gilmer、Conrad W. Hummel、Steven R. Jordan、Christopher Mohr、Lisa M. Shewchuk、Daniel D. Sternbach、Marc Rodriguez

  DOI：10.1021/jm970853a

  日期：1998.5.1

  The design, synthesis, and evaluation of dipeptide analogues as ligands for the pp60(c-src) SH2 domain are described. The critical binding interactions between Ac-Tyr-Glu-N(n-C5H11)(2) (2) and the protein are established and form the basis for our structure-based drug design efforts. The effects of changes in both the C-terminal (11-27) and N-terminal (51-69) portions of the dipeptide are explored. Analogues with reduced overall charge (92-95) are also investigated. We demonstrate the feasibility of pairing structurally diverse subunits in a modest dipeptide framework with the goal of increasing the druglike attributes without sacrificing binding affinity.