α-methyl β-pentafluorophenyl (2R,3S)-N-Boc-3-methyl-aspartate | 181590-13-6

• 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: α-methyl β-pentafluorophenyl (2R,3S)-N-Boc-3-methyl-aspartate
• 英文别名: 1-O-methyl 4-O-(2,3,4,5,6-pentafluorophenyl) (2R,3S)-3-methyl-2-[(2-methylpropan-2-yl)oxycarbonylamino]butanedioate
• CAS: 181590-13-6
• 化学式: C₁₇H₁₈F₅NO₆
• 分子量: 427.325
• InChiKey: JVBTVYFWYUASMG-PWCHPLFNSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.3
• 重原子数：
  29
• 可旋转键数：
  9
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.47
• 拓扑面积：
  90.9
• 氢给体数：
  1
• 氢受体数：
  11

反应信息

• 作为反应物：
  描述：

  α-methyl β-pentafluorophenyl (2R,3S)-N-Boc-3-methyl-aspartate 在 2,3,5-三甲基吡啶 、 盐酸 、 4-二甲氨基吡啶 、 N,N-二异丙基乙胺 、 三氟乙酸 、 N-[(dimethylamino)-3-oxo-1H-1,2,3-triazolo[4,5-b]pyridin-1-yl-methylene]-N-methylmethanaminium hexafluorophosphate 作用下， 以 四氢呋喃 、 乙醚 、 二氯甲烷 、 N,N-二甲基甲酰胺 为溶剂， 反应 117.0h， 生成 3-(1-allyloxycarbonyl-2-methyl-propylcarbamoyl)-2-(2-{[4-(3-tert-butoxycarbonylamino-9-methoxy-2,6,8-trimethyl-10-phenyl-deca-4,6-dienoylamino)-4-methoxycarbonyl-butyryl]-methyl-amino}-3-hydroxy-butyrylamino)-butyric acid methyl ester
  参考文献：
  名称：

  Total Synthesis of Motuporin and 5-[l-Ala]-Motuporin

  摘要：

  Total synthesis of the cyclic peptide hepatotoxin motuporin is described, including an efficient synthesis of the constituent amino acid Adda. Three strategies to motuporin are outlined with their relative strengths and weaknesses. Cyclization of the linear peptide precursor was found to proceed moderately well for peptides containing the N-methyldehydrobutyrine residue masked as a threonine, but significant C-terminal epimerization occurred in the presence of the dehydroamino acid. Replacement of the N-methyldehydrobutyrine residue by L-alanine was explored to assess the contribution of this dehydroamino acid to the biochemical activity of motuporin. Some epimerization also was observed during cyclization of the alanine-containing peptide. Synthetic motuporin and both isomers of 5-[L-Ala]-motuporin inhibit the activity of protein phosphatase-l (PP1) in rat adipocyte lysates with comparable IC50 values. These results indicate that the N-methyldehydrobutyrine residue is not essential for PP1 inhibition.

  DOI：

  10.1021/jo982145i
• 作为产物：
  描述：

  五氟苯酚 、 methyl(2S,3R)-3-tert-butoxycarbonylamino-4-methoxycarbonyl-3-methylbutanoic acid 在 4-二甲氨基吡啶 、 N,N'-二环己基碳二亚胺 作用下， 以 二氯甲烷 为溶剂， 以85%的产率得到α-methyl β-pentafluorophenyl (2R,3S)-N-Boc-3-methyl-aspartate
  参考文献：
  名称：

  Total Synthesis of Motuporin and 5-[l-Ala]-Motuporin

  摘要：

  Total synthesis of the cyclic peptide hepatotoxin motuporin is described, including an efficient synthesis of the constituent amino acid Adda. Three strategies to motuporin are outlined with their relative strengths and weaknesses. Cyclization of the linear peptide precursor was found to proceed moderately well for peptides containing the N-methyldehydrobutyrine residue masked as a threonine, but significant C-terminal epimerization occurred in the presence of the dehydroamino acid. Replacement of the N-methyldehydrobutyrine residue by L-alanine was explored to assess the contribution of this dehydroamino acid to the biochemical activity of motuporin. Some epimerization also was observed during cyclization of the alanine-containing peptide. Synthetic motuporin and both isomers of 5-[L-Ala]-motuporin inhibit the activity of protein phosphatase-l (PP1) in rat adipocyte lysates with comparable IC50 values. These results indicate that the N-methyldehydrobutyrine residue is not essential for PP1 inhibition.

  DOI：

  10.1021/jo982145i

文献信息

• Total Synthesis of Motuporin and 5-[<scp>l</scp>-Ala]-Motuporin
  作者：Raghu Samy、Hong Yong Kim、Matthew Brady、Peter L. Toogood

  DOI：10.1021/jo982145i

  日期：1999.4.1

  Total synthesis of the cyclic peptide hepatotoxin motuporin is described, including an efficient synthesis of the constituent amino acid Adda. Three strategies to motuporin are outlined with their relative strengths and weaknesses. Cyclization of the linear peptide precursor was found to proceed moderately well for peptides containing the N-methyldehydrobutyrine residue masked as a threonine, but significant C-terminal epimerization occurred in the presence of the dehydroamino acid. Replacement of the N-methyldehydrobutyrine residue by L-alanine was explored to assess the contribution of this dehydroamino acid to the biochemical activity of motuporin. Some epimerization also was observed during cyclization of the alanine-containing peptide. Synthetic motuporin and both isomers of 5-[L-Ala]-motuporin inhibit the activity of protein phosphatase-l (PP1) in rat adipocyte lysates with comparable IC50 values. These results indicate that the N-methyldehydrobutyrine residue is not essential for PP1 inhibition.