methyl (7S)-7-amino-8-oxo-8-(2-phenylethylamino)octanoate | 1528755-37-4

• 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 (7S)-7-amino-8-oxo-8-(2-phenylethylamino)octanoate
• CAS: 1528755-37-4
• 化学式: C₁₇H₂₆N₂O₃
• 分子量: 306.405
• InChiKey: XQTHQAZVACOXAJ-HNNXBMFYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.8
• 重原子数：
  22.0
• 可旋转键数：
  10.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.53
• 拓扑面积：
  81.42
• 氢给体数：
  2.0
• 氢受体数：
  4.0

反应信息

• 作为反应物：
  描述：

  methyl (7S)-7-amino-8-oxo-8-(2-phenylethylamino)octanoate 在 N-甲基吗啉 、 羟胺 、 4-(4,6-二甲氧基三嗪-2-基)-4-甲基吗啉盐酸盐 、 sodium hydroxide 作用下， 以 四氢呋喃 、 甲醇 、 水 为溶剂， 反应 24.0h， 生成 (2S)-N'-hydroxy-2-[[(2S)-5-oxopyrrolidine-2-carbonyl]amino]-N-(2-phenylethyl)octanediamide
  参考文献：
  名称：

  Lactam based 7-amino suberoylamide hydroxamic acids as potent HDAC inhibitors

  摘要：

  A series of SAHA-like molecules were prepared introducing different lactam-carboxyamides in position 7 of the suberoylanilide skeleton. The activity against different HDAC isoforms was tested and the data compared with the corresponding linear products, without substituent in position 7. In general, this modification provided an effective reinforcement of in vitro activity. While the lactam size or the CO/NH group orientation did not strongly influence the inhibition, the contemporary modification of the suberoylamide fragment gave vary active variants in the lactam series, with compound 28 (ST8078AA1) that showed IC50 values between 2 and 10 nM against all Class I HDAC isoforms, demonstrating it to be a large spectrum pan-inhibitor. This strong affinity with HDAC was also confirmed by the value of IC50 = 0.5 mu M against H460 cells, ranking 28 as one of the most potent HDAC inhibitors described so far. (C) 2013 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2013.11.072
• 作为产物：
  描述：

  在 三氟乙酸 作用下， 以 二氯甲烷 为溶剂， 反应 1.0h， 生成 methyl (7S)-7-amino-8-oxo-8-(2-phenylethylamino)octanoate
  参考文献：
  名称：

  Lactam based 7-amino suberoylamide hydroxamic acids as potent HDAC inhibitors

  摘要：

  A series of SAHA-like molecules were prepared introducing different lactam-carboxyamides in position 7 of the suberoylanilide skeleton. The activity against different HDAC isoforms was tested and the data compared with the corresponding linear products, without substituent in position 7. In general, this modification provided an effective reinforcement of in vitro activity. While the lactam size or the CO/NH group orientation did not strongly influence the inhibition, the contemporary modification of the suberoylamide fragment gave vary active variants in the lactam series, with compound 28 (ST8078AA1) that showed IC50 values between 2 and 10 nM against all Class I HDAC isoforms, demonstrating it to be a large spectrum pan-inhibitor. This strong affinity with HDAC was also confirmed by the value of IC50 = 0.5 mu M against H460 cells, ranking 28 as one of the most potent HDAC inhibitors described so far. (C) 2013 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2013.11.072