ethyl (1R,2S)-1,2-diphenylcyclopropanecarboxylate

• 分子结构分类: 有机化合物 - 苯丙烷和聚酮 - 二苯乙烯类
• 英文名称: ethyl (1R,2S)-1,2-diphenylcyclopropanecarboxylate
• 英文别名: 1,2-diphenylethyl ester (1R,2S)-cyclopropanecarboxylic acid；ethyl (1R,2S)-1,2-diphenylcyclopropane-1-carboxylate
• 化学式: C₁₈H₁₈O₂
• 分子量: 266.34
• InChiKey: AKJUISUOAGMHAI-WMZOPIPTSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.8
• 重原子数：
  20
• 可旋转键数：
  5
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.28
• 拓扑面积：
  26.3
• 氢给体数：
  0
• 氢受体数：
  2

反应信息

• 作为反应物：
  描述：

  ethyl (1R,2S)-1,2-diphenylcyclopropanecarboxylate 在 水 、 lithium hydroxide 作用下， 以 四氢呋喃 、 乙醇 为溶剂， 反应 1.0h， 以67%的产率得到(1R,2S)-1,2-diphenylcyclopropanecarboxylic acid
  参考文献：
  名称：

  Synthesis, biological activity and mechanistic insights of 1-substituted cyclopropylamine derivatives: A novel class of irreversible inhibitors of histone demethylase KDM1A

  摘要：

  Histone demethylase KDM1A (also known as LSD1) has become an attractive therapeutic target for the treatment of cancer as well as other disorders such as viral infections. We report on the synthesis of compounds derived from the expansion of tranylcypromine as a chemical scaffold for the design of novel demethylase inhibitors. These compounds, which are substituted on the cyclopropyl core moiety, were evaluated for their ability to inhibit KDM1A in vitro as well as to function in cells by modulating the expression of Gfi-1b, a well recognized KDM1A target gene. The molecules were all found to covalently inhibit KDM1A and to become increasingly selective against human monoamine oxidases MAO A and MAO B through the introduction of bulkier substituents on the cyclopropylamine ring. Structural and biochemical analysis of selected trans isomers showed that the two stereoisomers are endowed with similar inhibitory activities against KDM1A, but form different covalent adducts with the FAD co-enzyme. (C) 2014 Elsevier Masson SAS. All rights reserved.

  DOI：

  10.1016/j.ejmech.2014.08.068
• 作为产物：
  描述：

  ethyl 2-diethoxyphosphoryl-2-phenylacetate 、 (S)-环氧苯乙烷 在 正丁基锂 作用下， 以 乙二醇二甲醚 为溶剂， 反应 1.91h， 以100%的产率得到ethyl (1R,2S)-1,2-diphenylcyclopropanecarboxylate
  参考文献：
  名称：

  Synthesis, biological activity and mechanistic insights of 1-substituted cyclopropylamine derivatives: A novel class of irreversible inhibitors of histone demethylase KDM1A

  摘要：

  Histone demethylase KDM1A (also known as LSD1) has become an attractive therapeutic target for the treatment of cancer as well as other disorders such as viral infections. We report on the synthesis of compounds derived from the expansion of tranylcypromine as a chemical scaffold for the design of novel demethylase inhibitors. These compounds, which are substituted on the cyclopropyl core moiety, were evaluated for their ability to inhibit KDM1A in vitro as well as to function in cells by modulating the expression of Gfi-1b, a well recognized KDM1A target gene. The molecules were all found to covalently inhibit KDM1A and to become increasingly selective against human monoamine oxidases MAO A and MAO B through the introduction of bulkier substituents on the cyclopropylamine ring. Structural and biochemical analysis of selected trans isomers showed that the two stereoisomers are endowed with similar inhibitory activities against KDM1A, but form different covalent adducts with the FAD co-enzyme. (C) 2014 Elsevier Masson SAS. All rights reserved.

  DOI：

  10.1016/j.ejmech.2014.08.068

文献信息

• Alkoxydiaminophosphine Ligands as Surrogates of NHCs in Copper Catalysis
  作者：Juan Diego Pizarro、Francisco Molina、Manuel R. Fructos、Pedro J. Pérez

  DOI：10.1002/chem.202001517

  日期：2020.8.12

  A family of phosphine ligands containing a five‐membered ring similar to the popular N‐heterocyclic carbene ligands and an alkoxy third substituent has been developed. These alkoxydiaminophosphine ligands (ADAP) can be generated in one pot and reacted with a copper(I) source leading to the high yield isolation of complexes [(ADAP)CuX]2 (X=Cl, Br). The dinuclear nature of these compounds has been established

  已开发出一个含有五元环的膦配体，该环类似于流行的N杂环卡宾配体，并带有一个烷氧基第三取代基。这些烷氧基二氨基膦配体（ADAP）可以在一个锅中生成，并与铜（I）源反应，从而导致复合物[（ADAP）CuX] 2的高产率分离。（X ＝ Cl，Br）。这些化合物的双核性质已通过X射线研究和DOSY实验确定。对这些配合物从重氮化合物到CH键（烷烃，芳烃），烯烃或NH键的卡宾转移反应的催化性能的筛选，以及在CuAAC或腈转移反应中的性能至少相似（如果不是更好的话），则比他们的（NHC）CuCl类似物好，这些易于调节的ADAP配体为铜催化打开了一个新窗口。
• Sidearm effects in the enantioselective cyclopropanation of alkenes with aryldiazoacetates catalyzed by trisoxazoline/Cu(i)
  作者：Zheng-Hu Xu、Sha-Na Zhu、Xiu-Li Sun、Yong Tang、Li-Xin Dai

  DOI：10.1039/b617967c

  日期：——

  A highly enantioselective cyclopropanation of alkenes with phenyldiazoacetates catalyzed by CuPF6(CH3CN)4/trisoxazoline has been developed.

  已开发出一种由 CuPF6(CH3CN)4/三恶唑啉催化的烯烃与重氮乙酸苯基酯的高度对映选择性环丙烷化反应。
• Synthesis, biological activity and mechanistic insights of 1-substituted cyclopropylamine derivatives: A novel class of irreversible inhibitors of histone demethylase KDM1A
  作者：Paola Vianello、Oronza A. Botrugno、Anna Cappa、Giuseppe Ciossani、Paola Dessanti、Antonello Mai、Andrea Mattevi、Giuseppe Meroni、Saverio Minucci、Florian Thaler、Marcello Tortorici、Paolo Trifiró、Sergio Valente、Manuela Villa、Mario Varasi、Ciro Mercurio

  DOI：10.1016/j.ejmech.2014.08.068

  日期：2014.10

  Histone demethylase KDM1A (also known as LSD1) has become an attractive therapeutic target for the treatment of cancer as well as other disorders such as viral infections. We report on the synthesis of compounds derived from the expansion of tranylcypromine as a chemical scaffold for the design of novel demethylase inhibitors. These compounds, which are substituted on the cyclopropyl core moiety, were evaluated for their ability to inhibit KDM1A in vitro as well as to function in cells by modulating the expression of Gfi-1b, a well recognized KDM1A target gene. The molecules were all found to covalently inhibit KDM1A and to become increasingly selective against human monoamine oxidases MAO A and MAO B through the introduction of bulkier substituents on the cyclopropylamine ring. Structural and biochemical analysis of selected trans isomers showed that the two stereoisomers are endowed with similar inhibitory activities against KDM1A, but form different covalent adducts with the FAD co-enzyme. (C) 2014 Elsevier Masson SAS. All rights reserved.