(R)-ethyl 2-tert-butoxycarbonylaminohept-6-enoate | 1150697-95-2

• 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: (R)-ethyl 2-tert-butoxycarbonylaminohept-6-enoate
• 英文别名: ethyl (2R)-2-[(2-methylpropan-2-yl)oxycarbonylamino]hept-6-enoate
• CAS: 1150697-95-2
• 化学式: C₁₄H₂₅NO₄
• 分子量: 271.357
• InChiKey: OCRLWXMPHXIASF-LLVKDONJSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.1
• 重原子数：
  19
• 可旋转键数：
  10
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.71
• 拓扑面积：
  64.6
• 氢给体数：
  1
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  (R)-ethyl 2-tert-butoxycarbonylaminohept-6-enoate 在 乙醇 、 sodium hydroxide 作用下， 反应 4.0h， 以99%的产率得到(R)-2-tert-butoxycarbonylamino-hept-6-enoic acid
  参考文献：
  名称：

  Bicyclic tetrapeptides as potent HDAC inhibitors: Effect of aliphatic loop position and hydrophobicity on inhibitory activity

  摘要：

  Several histone deacetylase (HDAC) inhibiting bicyclic tetrapeptides have been designed and synthesized through intramolecular ring-closing metathesis (RCM) reaction and peptide cyclization. We designed bicyclic tetrapeptides based on CHAP31, trapoxin B and HC-toxin I. The HDAC inhibitory and p21 promoter assay results showed that the aliphatic loop position as well as the hydrophobicity plays an important role toward the activity of the bicyclic tetrapeptide HDAC inhibitors.

  DOI：

  10.1016/j.bmc.2014.06.031
• 作为产物：
  描述：

  二乙基(Boc-氨基)乙酯 在 ammonium hydroxide 、 水 、 sodium 、 sodium hydroxide 、 subtilisin Carlsberg from Bacillus licheniformis 作用下， 以 乙醇 、 N,N-二甲基甲酰胺 、 甲苯 为溶剂， 反应 17.5h， 生成 (R)-ethyl 2-tert-butoxycarbonylaminohept-6-enoate
  参考文献：
  名称：

  Bicyclic tetrapeptides as potent HDAC inhibitors: Effect of aliphatic loop position and hydrophobicity on inhibitory activity

  摘要：

  Several histone deacetylase (HDAC) inhibiting bicyclic tetrapeptides have been designed and synthesized through intramolecular ring-closing metathesis (RCM) reaction and peptide cyclization. We designed bicyclic tetrapeptides based on CHAP31, trapoxin B and HC-toxin I. The HDAC inhibitory and p21 promoter assay results showed that the aliphatic loop position as well as the hydrophobicity plays an important role toward the activity of the bicyclic tetrapeptide HDAC inhibitors.

  DOI：

  10.1016/j.bmc.2014.06.031

文献信息

• Design, Synthesis, and Biological Activity of Boronic Acid-Based Histone Deacetylase Inhibitors
  作者：Nobuaki Suzuki、Takayoshi Suzuki、Yosuke Ota、Tatsuya Nakano、Masaaki Kurihara、Haruhiro Okuda、Takao Yamori、Hiroki Tsumoto、Hidehiko Nakagawa、Naoki Miyata

  DOI：10.1021/jm900125m

  日期：2009.5.14

  Guided by the proposed catalytic mechanism of histone deacetylases (HDACs), we designed and synthesized a series of boronic acid-based HDAC inhibitors bearing an alpha-amino acid moiety. In this series, compounds (S)-18, 20, and 21 showed potent HDAC-inhibitory activity, highlighting the significance of the (S)-amino acid moiety. In cancer cell growth inhibition assays, compounds (S)-18. 20, and 21 exerted strong activity, and the values of the ratio of the concentration causing 50% growth inhibition (GI(50)) to the concentration causing 50% enzyme inhibition (IC50), i.e., GI(50)/IC50, were low. The potency of these compounds was similar to that of clinically used suberoylanilide hydroxamic acid (SAHA) (2). The results of Western blot analysis indicated that the-cancer cell growth-inhibitory activity of compounds (S)-18, 20, and 21 is the result of HDAC inhibition. A molecular modeling study suggested that the hydrated boronic acid interacts with zinc ion, Tyr residue, and His residue in the active site of HDACs. Our findings indicate that these boronic acid derivatives represent an entry into a new class of HDAC inhibitors.
• Bicyclic tetrapeptides as potent HDAC inhibitors: Effect of aliphatic loop position and hydrophobicity on inhibitory activity
  作者：Md. Nurul Islam、Md. Shahidul Islam、Md. Ashraful Hoque、Tamaki Kato、Norikazu Nishino、Akihiro Ito、Minoru Yoshida

  DOI：10.1016/j.bmc.2014.06.031

  日期：2014.8

  Several histone deacetylase (HDAC) inhibiting bicyclic tetrapeptides have been designed and synthesized through intramolecular ring-closing metathesis (RCM) reaction and peptide cyclization. We designed bicyclic tetrapeptides based on CHAP31, trapoxin B and HC-toxin I. The HDAC inhibitory and p21 promoter assay results showed that the aliphatic loop position as well as the hydrophobicity plays an important role toward the activity of the bicyclic tetrapeptide HDAC inhibitors.