(4S)-4-propan-2-yl-3-[(2S)-2-(4-propan-2-ylphenyl)propanoyl]-1,3-oxazolidin-2-one | 222737-10-2

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 异戊烯醇脂质
• 英文名称: (4S)-4-propan-2-yl-3-[(2S)-2-(4-propan-2-ylphenyl)propanoyl]-1,3-oxazolidin-2-one
• CAS: 222737-10-2
• 化学式: C₁₈H₂₅NO₃
• 分子量: 303.401
• InChiKey: HTILAMYEHWWMHQ-XJKSGUPXSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.4
• 重原子数：
  22
• 可旋转键数：
  4
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.56
• 拓扑面积：
  46.6
• 氢给体数：
  0
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  (4S)-4-propan-2-yl-3-[(2S)-2-(4-propan-2-ylphenyl)propanoyl]-1,3-oxazolidin-2-one 在 palladium on activated charcoal lithium hydroxide 、 二苯基膦叠氮化物 、 氢气 、 双氧水 、 三乙胺 作用下， 以 四氢呋喃 、 乙醇 为溶剂， -30.0~25.0 ℃ 、101.33 kPa 条件下， 反应 22.75h， 生成 [4-[(2S)-2-acetamido-3-[[(2S)-4-methyl-1-oxo-1-[[(1S)-1-(4-propan-2-ylphenyl)ethyl]amino]pentan-2-yl]amino]-3-oxopropyl]phenyl] dihydrogen phosphate
  参考文献：
  名称：

  Phosphotyrosine-Containing Dipeptides as High-Affinity Ligands for the p56^lck SH2 Domain

  摘要：

  Src homology-2 (SH2) domains are noncatalytic motifs containing approximately 100 amino acid residues that are involved in intracellular signal transduction. The phosphotyrosine-containing tetrapeptide Ac-pYEEI binds to the SH2 domain of p.56(lck) (Lck) with an affinity of 0.1 mu M. Starting from Ac-pYEEI, we have designed potent antagonists of the Lck SH2 domain which are reduced in peptidic character and in which the three carboxyl groups have been eliminated. The two C-terminal amino acids (EI) have been replaced by benzylamine derivatives and the pY + 1 glutamic acid has been substituted with leucine. The best C-terminal fragment identified, (S)-1-(4-isopropylphenyl)ethylamine, binds to the Lck SH2 domain better than the C-terminal dipeptide EI. Molecular modeling suggests that the substituents at the 4-position of the phenyl ring occupy the pY + 3 lipophilic pocket in the SH2 domain originally occupied by the isoleucine side chain. This new series of phosphotyrosine-containing dipeptides binds to the Lck SH2 domain with potencies comparable to that of tetrapeptide 1.

  DOI：

  10.1021/jm980612i
• 作为产物：
  描述：

  4-isopropylphenylacetyl chloride 在 正丁基锂 、 lithium hexamethyldisilazane 作用下， 反应 3.5h， 生成 (4S)-4-propan-2-yl-3-[(2S)-2-(4-propan-2-ylphenyl)propanoyl]-1,3-oxazolidin-2-one
  参考文献：
  名称：

  Phosphotyrosine-Containing Dipeptides as High-Affinity Ligands for the p56^lck SH2 Domain

  摘要：

  Src homology-2 (SH2) domains are noncatalytic motifs containing approximately 100 amino acid residues that are involved in intracellular signal transduction. The phosphotyrosine-containing tetrapeptide Ac-pYEEI binds to the SH2 domain of p.56(lck) (Lck) with an affinity of 0.1 mu M. Starting from Ac-pYEEI, we have designed potent antagonists of the Lck SH2 domain which are reduced in peptidic character and in which the three carboxyl groups have been eliminated. The two C-terminal amino acids (EI) have been replaced by benzylamine derivatives and the pY + 1 glutamic acid has been substituted with leucine. The best C-terminal fragment identified, (S)-1-(4-isopropylphenyl)ethylamine, binds to the Lck SH2 domain better than the C-terminal dipeptide EI. Molecular modeling suggests that the substituents at the 4-position of the phenyl ring occupy the pY + 3 lipophilic pocket in the SH2 domain originally occupied by the isoleucine side chain. This new series of phosphotyrosine-containing dipeptides binds to the Lck SH2 domain with potencies comparable to that of tetrapeptide 1.

  DOI：

  10.1021/jm980612i

文献信息

• Phosphotyrosine-Containing Dipeptides as High-Affinity Ligands for the p56<i>^lck</i> SH2 Domain
  作者：Montse Llinàs-Brunet、Pierre L. Beaulieu、Dale R. Cameron、Jean-Marie Ferland、Jean Gauthier、Elise Ghiro、James Gillard、Vida Gorys、Martin Poirier、Jean Rancourt、Dominik Wernic、Raj Betageri、Mario Cardozo、Scott Jakes、Suzanne Lukas、Usha Patel、John Proudfoot、Neil Moss

  DOI：10.1021/jm980612i

  日期：1999.2.1

  Src homology-2 (SH2) domains are noncatalytic motifs containing approximately 100 amino acid residues that are involved in intracellular signal transduction. The phosphotyrosine-containing tetrapeptide Ac-pYEEI binds to the SH2 domain of p.56(lck) (Lck) with an affinity of 0.1 mu M. Starting from Ac-pYEEI, we have designed potent antagonists of the Lck SH2 domain which are reduced in peptidic character and in which the three carboxyl groups have been eliminated. The two C-terminal amino acids (EI) have been replaced by benzylamine derivatives and the pY + 1 glutamic acid has been substituted with leucine. The best C-terminal fragment identified, (S)-1-(4-isopropylphenyl)ethylamine, binds to the Lck SH2 domain better than the C-terminal dipeptide EI. Molecular modeling suggests that the substituents at the 4-position of the phenyl ring occupy the pY + 3 lipophilic pocket in the SH2 domain originally occupied by the isoleucine side chain. This new series of phosphotyrosine-containing dipeptides binds to the Lck SH2 domain with potencies comparable to that of tetrapeptide 1.