tert-butyl N-[(2S)-1-[[(2S)-1-(dipentylamino)-4-methylsulfanyl-1-oxobutan-2-yl]amino]-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]carbamate | 205236-93-7

• 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: tert-butyl N-[(2S)-1-[[(2S)-1-(dipentylamino)-4-methylsulfanyl-1-oxobutan-2-yl]amino]-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]carbamate
• CAS: 205236-93-7
• 化学式: C₂₉H₄₉N₃O₅S
• 分子量: 551.791
• InChiKey: UGYCBDMUNMMPSB-DQEYMECFSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  6.1
• 重原子数：
  38
• 可旋转键数：
  19
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.69
• 拓扑面积：
  133
• 氢给体数：
  3
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  tert-butyl N-[(2S)-1-[[(2S)-1-(dipentylamino)-4-methylsulfanyl-1-oxobutan-2-yl]amino]-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]carbamate 在 盐酸 、 1-羟基苯并三唑 、 三乙胺 、 N,N'-二环己基碳二亚胺 作用下， 以 1,4-二氧六环 、 二氯甲烷 、 N,N-二甲基甲酰胺 为溶剂， 反应 21.0h， 生成 (2S)-2-[[(2S)-2-acetamido-3-(4-hydroxyphenyl)propanoyl]amino]-4-methylsulfanyl-N,N-dipentylbutanamide
  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：

  Boc-L-蛋氨酸 在 N-甲基吗啉 、 盐酸 、 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 、 1,4-二氧六环 、 二氯甲烷 、 N,N-二甲基甲酰胺 为溶剂， 反应 33.58h， 生成 tert-butyl N-[(2S)-1-[[(2S)-1-(dipentylamino)-4-methylsulfanyl-1-oxobutan-2-yl]amino]-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]carbamate
  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