Fmoc-Tyr(PO3Bn2)-Glu(OBn)-NHBn(4-OMe) | 229171-82-8

• 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: Fmoc-Tyr(PO3Bn2)-Glu(OBn)-NHBn(4-OMe)
• 英文别名: benzyl (4S)-4-[[(2S)-3-[4-bis(phenylmethoxy)phosphoryloxyphenyl]-2-(9H-fluoren-9-ylmethoxycarbonylamino)propanoyl]amino]-5-[(4-methoxyphenyl)methylamino]-5-oxopentanoate
• CAS: 229171-82-8
• 化学式: C₅₈H₅₆N₃O₁₁P
• 分子量: 1002.07
• InChiKey: AERJJMSCDLJIOQ-PJYGOTMFSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  9.3
• 重原子数：
  73
• 可旋转键数：
  26
• 环数：
  8.0
• sp3杂化的碳原子比例：
  0.21
• 拓扑面积：
  177
• 氢给体数：
  3
• 氢受体数：
  11

反应信息

• 作为反应物：
  描述：

  Fmoc-Tyr(PO3Bn2)-Glu(OBn)-NHBn(4-OMe) 在 1,8-二氮杂双环[5.4.0]十一碳-7-烯 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 0.25h， 生成 H-Tyr(PO3Bn2)-Glu(OBn)-NHBn(4-OMe)
  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 The two C-terminal amino acids (EI) have been replaced by benzylamine derivatives and the pY + 1 glutamic acid has been substituted with leucine.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-甲氧基苄胺 在 N-甲基吗啉 、 盐酸 、 O-(benzotriazol-1-yl)-N,N,N',N'-tetramethyluronium tetrafluoroborate 作用下， 以 1,4-二氧六环 为溶剂， 反应 0.92h， 生成 Fmoc-Tyr(PO3Bn2)-Glu(OBn)-NHBn(4-OMe)
  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.