Fmoc-(L)-Asu-OMe | 1416446-17-7

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯酚醚
• 英文名称: Fmoc-(L)-Asu-OMe
• CAS: 1416446-17-7
• 化学式: C₁₇H₂₄N₂O₅
• 分子量: 336.388
• InChiKey: TZLGFRTZEKKLMX-HNNXBMFYSA-N

物化性质

• 密度：
  1.162±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  1.67
• 重原子数：
  24.0
• 可旋转键数：
  10.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.53
• 拓扑面积：
  85.89
• 氢给体数：
  2.0
• 氢受体数：
  6.0

反应信息

• 作为反应物：
  描述：

  Fmoc-(L)-Asu-OMe 、 9-芴甲基-N-琥珀酰亚胺基碳酸酯 在 sodium hydroxide 、 碳酸氢钠 作用下， 以 四氢呋喃 、 水 、 丙酮 为溶剂， 反应 3.0h， 以60%的产率得到(L)-2-N-Fmoc-amino-7-(4-methoxy-benzyloxycarbamoyl)-heptanoic acid
  参考文献：
  名称：

  Solid phase synthesis of hydroxamate peptides for histone deacetylase inhibition

  摘要：

  An orthogonal protecting group strategy was devised to synthesize hydroxamic acid containing peptides for biomimetic histone deacetylase (HDAC) inhibition. The basic building block was a protected aminosuberic acid (Asu) derivative bearing a protected hydroxamate in the side-chain, related closely to HDAC inhibitors that are transition-state analogs of acetyllysine. These inhibitors include suberoylanilide hydroxamic acid (SAHA), currently being used to treat a variety of human cancers. This strategy was employed to synthesize a series of nonameric peptides related to actual HDAC substrates, derived from known sites of acetylation/deacetylation on the N-terminal tails of the histone core proteins H2A, H2B, H3, and H4. In each case the lysine residue was replaced by a hydroxamate-bearing side chain, to mimic the endogenous site of deacetylation. Mass spectrometry and high performance liquid chromatography (HPLC) confirmed the success of automated solid-phase synthesis. These results suggest facile synthesis of a new class of HDAC inhibitors that may have enhanced selectivity for specific HDAC isoforms. (C) 2012 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.tetlet.2012.10.113
• 作为产物：
  描述：

  4-甲氧基苄氧胺 、 在 草酰氯 、 N,N-二甲基甲酰胺 、 三乙胺 作用下， 以 二氯甲烷 为溶剂， 反应 3.0h， 以77%的产率得到Fmoc-(L)-Asu-OMe
  参考文献：
  名称：

  Solid phase synthesis of hydroxamate peptides for histone deacetylase inhibition

  摘要：

  An orthogonal protecting group strategy was devised to synthesize hydroxamic acid containing peptides for biomimetic histone deacetylase (HDAC) inhibition. The basic building block was a protected aminosuberic acid (Asu) derivative bearing a protected hydroxamate in the side-chain, related closely to HDAC inhibitors that are transition-state analogs of acetyllysine. These inhibitors include suberoylanilide hydroxamic acid (SAHA), currently being used to treat a variety of human cancers. This strategy was employed to synthesize a series of nonameric peptides related to actual HDAC substrates, derived from known sites of acetylation/deacetylation on the N-terminal tails of the histone core proteins H2A, H2B, H3, and H4. In each case the lysine residue was replaced by a hydroxamate-bearing side chain, to mimic the endogenous site of deacetylation. Mass spectrometry and high performance liquid chromatography (HPLC) confirmed the success of automated solid-phase synthesis. These results suggest facile synthesis of a new class of HDAC inhibitors that may have enhanced selectivity for specific HDAC isoforms. (C) 2012 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.tetlet.2012.10.113