(R)-3-(BOC-氨基)-5-(叔丁氧基)-5-氧代戊酸 | 128135-39-7

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 脂肪酰基
• 中文名称: (R)-3-(BOC-氨基)-5-(叔丁氧基)-5-氧代戊酸
• 英文名称: 3-<(tert-butoxycarbonyl)amino>pentanedioic acid 5-tert-butyl ester
• 英文别名: (R)-5-(tert-Butoxy)-3-((tert-butoxycarbonyl)amino)-5-oxopentanoic acid；(3R)-5-[(2-methylpropan-2-yl)oxy]-3-[(2-methylpropan-2-yl)oxycarbonylamino]-5-oxopentanoic acid
• CAS: 128135-39-7
• 化学式: C₁₄H₂₅NO₆
• 分子量: 303.356
• InChiKey: SJJQZIJVWBSAHD-SECBINFHSA-N

物化性质

• 沸点：
  449.8±40.0 °C(Predicted)
• 密度：
  1.121±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  1.3
• 重原子数：
  21
• 可旋转键数：
  9
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.79
• 拓扑面积：
  102
• 氢给体数：
  2
• 氢受体数：
  6

安全信息

• 危险性防范说明：
  P261,P280,P301+P312,P302+P352,P305+P351+P338
• 危险性描述：
  H302,H315,H319,H335

反应信息

• 作为反应物：
  描述：

  (R)-3-(BOC-氨基)-5-(叔丁氧基)-5-氧代戊酸 在 palladium on activated charcoal N-甲基吗啉 、 盐酸 、 氢气 、 三乙胺 、 氯甲酸异丁酯 作用下， 以 1,4-二氧六环 、 甲醇 、 水 为溶剂， -25.0~25.0 ℃ 、275.79 kPa 条件下， 反应 23.78h， 生成 [3-(N-acetylamino)-3-(carboxymethyl)propanoyl]-L-glutamic acid
  参考文献：
  名称：

  Synthesis of acyclic and dehydroaspartic acid analogs of Ac-Asp-Glu-OH and their inhibition of rat brain N-acetylated .alpha.-linked acidic dipeptidase (NAALA dipeptidase)

  摘要：

  The following structural and conformationally constrained analogues of Ac-Asp-Glu-OH (1) were synthesized: Ac-Glu-Glu-OH (2), Ac-D-Asp-Glu-OH (3), Ac-Glu-Asp-OH (4), Ac-Asp-Asp-OH (5), Ac-Asp-3-aminohexanedioic acid (6), Ac-3-amino-3-(carboxymethyl)propanoyl-Glu-OH (7), N-succinyl-Glu-OH (8), N-maleyl-Glu-OH (9), N-fumaryl-Glu-OH (10), and Ac-delta ZAsp-Glu-OH (11). These analogues were evaluated for their ability to inhibit the hydrolysis of Ac-Asp-[3,4-3H]-Glu-OH by N-acetylated alpha-linked acidic dipeptidase (NAALA dipeptidase) in order to gain some insight into the structural requirements for the inhibition of this enzyme. Analogues 4-6 and 9 were very weak inhibitors of NAALA dipeptidase (Ki greater than 40 microM), while 2, 3, and 7 with Ki values ranging from 3.2-8.5 microM showed intermediate inhibitory activity. The most active inhibitors of NAALA dipeptidase were compounds 8, 10, and 11 with Ki values of 0.9, 0.4, and 1.4 microM, respectively. These results suggest that the relative spacing between the side chain carboxyl and the alpha-carboxyl group of the C-terminal residue may be important for binding to the active site of the enzyme. They also indicate that the chi 1 torsional angle for the aspartyl residue is in the vicinity of 0 degrees.

  DOI：

  10.1021/jm00172a009
• 作为产物：
  描述：

  tert-butyl methyl 3-<(tert-butoxycarbonyl)amino>pentanedioate 在 sodium hydroxide 作用下， 以 甲醇 为溶剂， 反应 4.5h， 以96%的产率得到(R)-3-(BOC-氨基)-5-(叔丁氧基)-5-氧代戊酸
  参考文献：
  名称：

  Synthesis of acyclic and dehydroaspartic acid analogs of Ac-Asp-Glu-OH and their inhibition of rat brain N-acetylated .alpha.-linked acidic dipeptidase (NAALA dipeptidase)

  摘要：

  The following structural and conformationally constrained analogues of Ac-Asp-Glu-OH (1) were synthesized: Ac-Glu-Glu-OH (2), Ac-D-Asp-Glu-OH (3), Ac-Glu-Asp-OH (4), Ac-Asp-Asp-OH (5), Ac-Asp-3-aminohexanedioic acid (6), Ac-3-amino-3-(carboxymethyl)propanoyl-Glu-OH (7), N-succinyl-Glu-OH (8), N-maleyl-Glu-OH (9), N-fumaryl-Glu-OH (10), and Ac-delta ZAsp-Glu-OH (11). These analogues were evaluated for their ability to inhibit the hydrolysis of Ac-Asp-[3,4-3H]-Glu-OH by N-acetylated alpha-linked acidic dipeptidase (NAALA dipeptidase) in order to gain some insight into the structural requirements for the inhibition of this enzyme. Analogues 4-6 and 9 were very weak inhibitors of NAALA dipeptidase (Ki greater than 40 microM), while 2, 3, and 7 with Ki values ranging from 3.2-8.5 microM showed intermediate inhibitory activity. The most active inhibitors of NAALA dipeptidase were compounds 8, 10, and 11 with Ki values of 0.9, 0.4, and 1.4 microM, respectively. These results suggest that the relative spacing between the side chain carboxyl and the alpha-carboxyl group of the C-terminal residue may be important for binding to the active site of the enzyme. They also indicate that the chi 1 torsional angle for the aspartyl residue is in the vicinity of 0 degrees.

  DOI：

  10.1021/jm00172a009