H-Phe-c[-N^ε-Lys-Tyr-Abu-] | 403601-75-2

• 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: H-Phe-c[-N^ε-Lys-Tyr-Abu-]
• 英文别名: (2S)-2-amino-N-[(2S,14S)-2-[(4-hydroxyphenyl)methyl]-3,8,15-trioxo-1,4,9-triazacyclopentadec-14-yl]-3-phenylpropanamide
• CAS: 403601-75-2
• 化学式: C₂₈H₃₇N₅O₅
• 分子量: 523.632
• InChiKey: VISXYDOGUMZUMD-HJOGWXRNSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.4
• 重原子数：
  38
• 可旋转键数：
  6
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.43
• 拓扑面积：
  163
• 氢给体数：
  6
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  异丁烯 、 H-Phe-c[-N^ε-Lys-Tyr-Abu-] 在 三氟甲磺酸三甲基硅酯 、 三氟乙酸 作用下， 反应 12.0h， 以25%的产率得到(S)-2-Amino-N-[(2S,14S)-2-(3-tert-butyl-4-hydroxy-benzyl)-3,8,15-trioxo-1,4,9-triaza-cyclopentadec-14-yl]-3-phenyl-propionamide
  参考文献：
  名称：

  Design and Synthesis of Motilin Antagonists Derived from the [1−4] Fragment of Porcine Motilin

  摘要：

  A series of cyclic peptides having the general structure H-Phe-c[-N-epsilon-Lys-X-NH-(CH2)(n)-CO-] were designed on the basis of structure-activity relationship studies of motilin. All were motilin antagonists. The cyclic peptides, in which X is a 3-tert-butyl-substituted tyrosine residue (H-Phe-c[-N-epsilon-Lys-Tyr(3-tBu)-betaAla-] (3), H-Phe-c[-N-epsilon-Lys-Tyr(3-tBu)-Gly-] (6), H-Phe-c[-N-epsilon-Lys-Tyr(3-tBu)-Abu-] (7), and H-Phe-c[-N-epsilon-Lys-Tyr(3-tBu)-Ahx-] (8)) showed potent motilin receptor antagonistic activity in the rabbit smooth muscle (pA(2) > 7). The 3-tert-butyl Tyr was found to be the moiety responsible for enhanced binding to the motilin receptor, while the size of the ring had little importance.

  DOI：

  10.1021/jm010332u
• 作为产物：
  描述：

  4-[[(2S)-2-[[(2S)-6-amino-2-[[(2S)-2-(9H-fluoren-9-ylmethoxycarbonylamino)-3-phenylpropanoyl]amino]hexanoyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]butanoic acid 在 哌啶 、 吡啶 、 (benzotriazo-1-yloxy)tris(dimethylamino)phosphonium hexafluorophosphate 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 24.5h， 生成 H-Phe-c[-N^ε-Lys-Tyr-Abu-]
  参考文献：
  名称：

  Design and Synthesis of Motilin Antagonists Derived from the [1−4] Fragment of Porcine Motilin

  摘要：

  A series of cyclic peptides having the general structure H-Phe-c[-N-epsilon-Lys-X-NH-(CH2)(n)-CO-] were designed on the basis of structure-activity relationship studies of motilin. All were motilin antagonists. The cyclic peptides, in which X is a 3-tert-butyl-substituted tyrosine residue (H-Phe-c[-N-epsilon-Lys-Tyr(3-tBu)-betaAla-] (3), H-Phe-c[-N-epsilon-Lys-Tyr(3-tBu)-Gly-] (6), H-Phe-c[-N-epsilon-Lys-Tyr(3-tBu)-Abu-] (7), and H-Phe-c[-N-epsilon-Lys-Tyr(3-tBu)-Ahx-] (8)) showed potent motilin receptor antagonistic activity in the rabbit smooth muscle (pA(2) > 7). The 3-tert-butyl Tyr was found to be the moiety responsible for enhanced binding to the motilin receptor, while the size of the ring had little importance.

  DOI：

  10.1021/jm010332u