N-[3-(10H-phenothiazin-10-yl)propanoyl]methionine

• 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-[3-(10H-phenothiazin-10-yl)propanoyl]methionine
• 英文别名: (2S)-4-methylsulfanyl-2-(3-phenothiazin-10-ylpropanoylamino)butanoic acid
• 化学式: C₂₀H₂₂N₂O₃S₂
• 分子量: 402.538
• InChiKey: HGXLXQVWGBALSS-AWEZNQCLSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.6
• 重原子数：
  27
• 可旋转键数：
  8
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.3
• 拓扑面积：
  120
• 氢给体数：
  2
• 氢受体数：
  6

反应信息

• 作为产物：
  描述：

  1-{[3-(10H-phenothiazin-10-yl)propanoyl]oxy}pyrrolidine-2,5-dione 在 三乙胺 、 sodium hydroxide 作用下， 以 二氯甲烷 、 水 为溶剂， 反应 24.0h， 生成 N-[3-(10H-phenothiazin-10-yl)propanoyl]methionine
  参考文献：
  名称：

  Phenothiazine-based CaaX competitive inhibitors of human farnesyltransferase bearing a cysteine, methionine, serine or valine moiety as a new family of antitumoral compounds

  摘要：

  A new family of CaaX competitive inhibitors of human farnesyltransferase based on phenothiazine and carbazole skeleton bearing a L-cysteine, L-methionine, L-serine or L-valine moiety was designed, synthesized and biologically evaluated. Phenothiazine derivatives proved to be more active than carbazole-based compounds. Phenothiazine 1b with cysteine residue was the most promising inhibitor of human farnesyltransferase in the current study. (C) 2015 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2015.09.008

文献信息

• Phenothiazine-based CaaX competitive inhibitors of human farnesyltransferase bearing a cysteine, methionine, serine or valine moiety as a new family of antitumoral compounds
  作者：Gina-Mirabela Dumitriu、Elena Bîcu、Dalila Belei、Benoît Rigo、Joëlle Dubois、Amaury Farce、Alina Ghinet

  DOI：10.1016/j.bmcl.2015.09.008

  日期：2015.10

  A new family of CaaX competitive inhibitors of human farnesyltransferase based on phenothiazine and carbazole skeleton bearing a L-cysteine, L-methionine, L-serine or L-valine moiety was designed, synthesized and biologically evaluated. Phenothiazine derivatives proved to be more active than carbazole-based compounds. Phenothiazine 1b with cysteine residue was the most promising inhibitor of human farnesyltransferase in the current study. (C) 2015 Elsevier Ltd. All rights reserved.