methyl (2S)-3-[4-(2-cyclohexylethoxy)-3-iodophenyl]-2-(phenylmethoxycarbonylamino)propanoate | 204513-78-0

• 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: methyl (2S)-3-[4-(2-cyclohexylethoxy)-3-iodophenyl]-2-(phenylmethoxycarbonylamino)propanoate
• CAS: 204513-78-0
• 化学式: C₂₆H₃₂INO₅
• 分子量: 565.448
• InChiKey: QKWIGHXDTSWWMS-QHCPKHFHSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  7.1
• 重原子数：
  33
• 可旋转键数：
  12
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.46
• 拓扑面积：
  73.9
• 氢给体数：
  1
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  methyl (2S)-3-[4-(2-cyclohexylethoxy)-3-iodophenyl]-2-(phenylmethoxycarbonylamino)propanoate 在 palladium on activated charcoal N-甲基吗啉 、 咪唑 、 bis-triphenylphosphine-palladium(II) chloride 、 lithium hydroxide 、 copper(l) iodide 、 硼烷 、 氢气 、 溶剂黄146 、 三乙胺 作用下， 以 四氢呋喃 、 甲醇 、 乙醇 、 二氯甲烷 、 乙腈 为溶剂， -5.0~60.0 ℃ 、344.73 kPa 条件下， 反应 43.5h， 生成 tert-butyl N-[3-[5-[(2S)-2-amino-3-[tert-butyl(dimethyl)silyl]oxypropyl]-2-(2-cyclohexylethoxy)phenyl]propyl]carbamate
  参考文献：
  名称：

  Novel Biologically Active Nonpeptidic Inhibitors of MyristoylCoA:Protein N-Myristoyltransferase

  摘要：

  A new class of biologically active nonpeptidic inhibitors of Candida albicans NMT has been synthesized starting from the octapeptide ALYASKLS-NH2 (2). The synthetic strategy entailed the preparation of novel protected Ser-Lys mimics 9 and 12 from (S)- or (R)-3-iodotyrosine and then grafting key enzyme recognition elements in a stepwise manner. Like 2, compounds 16, 17, and 18 are competitive Candida NMT inhibitors that bind to the peptide recognition site of the enzyme. Moreover, 16-18 have an affinity comparable to that of 2 even though they are devoid of peptide bonds. In contrast to 2, these nonpeptidic inhibitors exhibit antifungal activity.

  DOI：

  10.1021/jm980001q
• 作为产物：
  描述：

  苯甲氧羰酰琥珀酰亚胺 在 N-甲基吗啉 、 四丁基氟化铵 作用下， 以 四氢呋喃 为溶剂， 反应 4.25h， 生成 methyl (2S)-3-[4-(2-cyclohexylethoxy)-3-iodophenyl]-2-(phenylmethoxycarbonylamino)propanoate
  参考文献：
  名称：

  Novel Biologically Active Nonpeptidic Inhibitors of MyristoylCoA:Protein N-Myristoyltransferase

  摘要：

  A new class of biologically active nonpeptidic inhibitors of Candida albicans NMT has been synthesized starting from the octapeptide ALYASKLS-NH2 (2). The synthetic strategy entailed the preparation of novel protected Ser-Lys mimics 9 and 12 from (S)- or (R)-3-iodotyrosine and then grafting key enzyme recognition elements in a stepwise manner. Like 2, compounds 16, 17, and 18 are competitive Candida NMT inhibitors that bind to the peptide recognition site of the enzyme. Moreover, 16-18 have an affinity comparable to that of 2 even though they are devoid of peptide bonds. In contrast to 2, these nonpeptidic inhibitors exhibit antifungal activity.

  DOI：

  10.1021/jm980001q