N-(tert-butyloxycarbonyl)-(γ-aminobutyryl)phenylalanine amide | 106651-43-8

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 肽模拟物
• 英文名称: N-(tert-butyloxycarbonyl)-(γ-aminobutyryl)phenylalanine amide
• CAS: 106651-43-8
• 化学式: C₁₈H₂₇N₃O₄
• 分子量: 349.43
• InChiKey: IQIIMFFVBOXSSI-AWEZNQCLSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.5
• 重原子数：
  25.0
• 可旋转键数：
  8.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.5
• 拓扑面积：
  110.52
• 氢给体数：
  3.0
• 氢受体数：
  4.0

反应信息

• 作为反应物：
  描述：

  N-(tert-butyloxycarbonyl)-(γ-aminobutyryl)phenylalanine amide 、 三氟乙酸 以 二氯甲烷 为溶剂， 反应 1.0h， 生成 (γ-aminobutyryl)phenylalanine amide TFA salt
  参考文献：
  名称：

  Synthesis and binding affinities of analogs of cholecystokinin-(30-33) as probes for central nervous system cholecystokinin receptors

  摘要：

  CCK-30-33 has been identified as the minimum fragment of CCK with nanomolar affinity for the central CCK receptors, as assayed by displacement of [3H]-Boc-beta-alanyl-CCK-30-33 (pentagastrin) in homogenized mouse cerebral cortex. Examination of binding using this assay in the two series Boc-Trp-X-Phe-NH2 when X = Met-Asp (Boc-CCK-30-33), Gly-Asp, Met-Gly, and Gly-Gly and when X = (CH2)n (n = 0-4) reveals that modification of the tetrapeptide reduces affinity to a maximum of micromolar affinity (Boc-Trp-Gly-Asp-Phe-NH2; Ki = 2 X 10(-6) M), whereas in the series when n = 0 and 2 pentamolar affinity is still retained (Boc-Trp-Phe-NH2, Ki = 7 X 10(-5) M; Boc-Trp NH CH2-CH2-CO-Phe-NH2, Ki = 3 X 10(-5) M). Modification of the tetrapeptide CCK-30-33 reduces affinity 1000-fold, whereas di- and tripeptide fragments are identified that reduce affinity only a further 10-fold. This structure-activity relationship establishes a basis to design "peptoid" analogues of CCK that have therapeutic potential.

  DOI：

  10.1021/jm00387a027
• 作为产物：
  描述：

  N-BOC-GAMMA-氨基丁酸 在 三乙胺 作用下， 以 四氢呋喃 、 水 为溶剂， 生成 N-(tert-butyloxycarbonyl)-(γ-aminobutyryl)phenylalanine amide
  参考文献：
  名称：

  Synthesis and binding affinities of analogs of cholecystokinin-(30-33) as probes for central nervous system cholecystokinin receptors

  摘要：

  CCK-30-33 has been identified as the minimum fragment of CCK with nanomolar affinity for the central CCK receptors, as assayed by displacement of [3H]-Boc-beta-alanyl-CCK-30-33 (pentagastrin) in homogenized mouse cerebral cortex. Examination of binding using this assay in the two series Boc-Trp-X-Phe-NH2 when X = Met-Asp (Boc-CCK-30-33), Gly-Asp, Met-Gly, and Gly-Gly and when X = (CH2)n (n = 0-4) reveals that modification of the tetrapeptide reduces affinity to a maximum of micromolar affinity (Boc-Trp-Gly-Asp-Phe-NH2; Ki = 2 X 10(-6) M), whereas in the series when n = 0 and 2 pentamolar affinity is still retained (Boc-Trp-Phe-NH2, Ki = 7 X 10(-5) M; Boc-Trp NH CH2-CH2-CO-Phe-NH2, Ki = 3 X 10(-5) M). Modification of the tetrapeptide CCK-30-33 reduces affinity 1000-fold, whereas di- and tripeptide fragments are identified that reduce affinity only a further 10-fold. This structure-activity relationship establishes a basis to design "peptoid" analogues of CCK that have therapeutic potential.

  DOI：

  10.1021/jm00387a027