Fmoc-D-Phe-Lys(1)-Tyr-bAla-(1) | 1026633-44-2

• 英文名称: Fmoc-D-Phe-Lys(1)-Tyr-bAla-(1)
• 英文别名: 9H-fluoren-9-ylmethyl N-[(2R)-1-[[(2S,13S)-2-[(4-hydroxyphenyl)methyl]-3,7,14-trioxo-1,4,8-triazacyclotetradec-13-yl]amino]-1-oxo-3-phenylpropan-2-yl]carbamate
• CAS: 1026633-44-2
• 化学式: C₄₂H₄₅N₅O₇
• 分子量: 731.849
• InChiKey: QXCBVADXASVVRP-AGSXMJPOSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.8
• 重原子数：
  54
• 可旋转键数：
  10
• 环数：
  6.0
• sp3杂化的碳原子比例：
  0.31
• 拓扑面积：
  175
• 氢给体数：
  6
• 氢受体数：
  7

反应信息

• 作为反应物：
  描述：

  Fmoc-D-Phe-Lys(1)-Tyr-bAla-(1) 在 哌啶 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 0.5h， 生成 H-D-Phe-c[-N^ε-Lys-Tyr-βAla-]
  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：

  Fmoc-D-Phe-Lys-Tyr-bAla-OH 在 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 24.0h， 生成 Fmoc-D-Phe-Lys(1)-Tyr-bAla-(1)
  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