(Z)-1-(3-cyanophenyl)-1-hexene | 945414-24-4

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: (Z)-1-(3-cyanophenyl)-1-hexene
• 英文别名: (Z)-1-(3-cyanophenyl)hex-1-ene；3-((Z)-hex-1-enyl)benzonitrile；3-[(Z)-hex-1-enyl]benzonitrile
• CAS: 945414-24-4
• 化学式: C₁₃H₁₅N
• 分子量: 185.269
• InChiKey: IVDLVBMNRHXKAX-ALCCZGGFSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.2
• 重原子数：
  14
• 可旋转键数：
  4
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.31
• 拓扑面积：
  23.8
• 氢给体数：
  0
• 氢受体数：
  1

反应信息

• 作为反应物：
  描述：

  (Z)-1-(3-cyanophenyl)-1-hexene 在 potassium tert-butylate 、 二异丁基氢化铝 作用下， 以 四氢呋喃 、 甲苯 为溶剂， 反应 17.25h， 生成
  参考文献：
  名称：

  Structure−Activity Relationships of α-Ketooxazole Inhibitors of Fatty Acid Amide Hydrolase

  摘要：

  A systematic study of the structure-activity relationships of 2b (OL-135), a potent inhibitor of fatty acid amide hydrolase (FAAH), is detailed targeting the C2 acyl side chain. A series of aryl replacements or substituents for the terminal phenyl group provided effective inhibitors (e.g., 5c, aryl = 1- napthyl, K-i = 2.6 nM), with 5hh (aryl = 3-ClPh, K-i = 900 pM) being 5-fold more potent than 2b. Conformationally restricted C2 side chains were examined, and many provided exceptionally potent inhibitors, of which 11j (ethylbiphenyl side chain) was established to be a 750 pM inhibitor. A systematic series of heteroatoms (O, NMe, S), electron-withdrawing groups (SO, SO2), and amides positioned within and hydroxyl substitutions on the linking side chain were investigated, which typically led to a loss in potency. The most tolerant positions provided effective inhibitors (12p, 6-position S, K-i = 3 nM, or 13d, 2-position OH, K-i = 8 nM) comparable in potency to 2b. Proteome-wide screening of selected inhibitors from the systematic series of > 100 candidates prepared revealed that they are selective for FAAH over all other mammalian serine proteases.

  DOI：

  10.1021/jm061414r
• 作为产物：
  描述：

  3-氰基苯甲醛 、 (1-戊基)三苯基溴化磷 在 正丁基锂 作用下， 以 四氢呋喃 为溶剂， 以86%的产率得到(Z)-1-(3-cyanophenyl)-1-hexene
  参考文献：
  名称：

  Structure−Activity Relationships of α-Ketooxazole Inhibitors of Fatty Acid Amide Hydrolase

  摘要：

  A systematic study of the structure-activity relationships of 2b (OL-135), a potent inhibitor of fatty acid amide hydrolase (FAAH), is detailed targeting the C2 acyl side chain. A series of aryl replacements or substituents for the terminal phenyl group provided effective inhibitors (e.g., 5c, aryl = 1- napthyl, K-i = 2.6 nM), with 5hh (aryl = 3-ClPh, K-i = 900 pM) being 5-fold more potent than 2b. Conformationally restricted C2 side chains were examined, and many provided exceptionally potent inhibitors, of which 11j (ethylbiphenyl side chain) was established to be a 750 pM inhibitor. A systematic series of heteroatoms (O, NMe, S), electron-withdrawing groups (SO, SO2), and amides positioned within and hydroxyl substitutions on the linking side chain were investigated, which typically led to a loss in potency. The most tolerant positions provided effective inhibitors (12p, 6-position S, K-i = 3 nM, or 13d, 2-position OH, K-i = 8 nM) comparable in potency to 2b. Proteome-wide screening of selected inhibitors from the systematic series of > 100 candidates prepared revealed that they are selective for FAAH over all other mammalian serine proteases.

  DOI：

  10.1021/jm061414r

文献信息

• A Highly Efficient and Recyclable Pd(Pph₃)₄/Peg-400 System for Stille Cross-Coupling Reactions of Organostannanes with Aryl Bromides
  作者：Xue Huang、Fang Yao、Ting Wei、Mingzhong Cai

  DOI：10.3184/174751917x15045169836226

  日期：2017.9

  Pd(PPh3)4 in PEG-400 is shown to be a highly efficient catalyst for the Stille cross-coupling reactions of various organotin compounds with aryl bromides. The reaction could be conducted at 80 °C using NaOAc as base, yielding a variety of biaryls, alkynes and alkenes in good to excellent yields. The isolation of the products was readily performed by extraction with petroleum ether and the Pd(PPh3)4/PEG-400

  PEG-400 中的 Pd(PPh3)4 被证明是各种有机锡化合物与芳基溴化物的 Stille 交叉偶联反应的高效催化剂。该反应可以在 80 °C 下使用 NaOAc 作为碱进行，以良好到极好的收率产生各种联芳基化合物、炔烃和烯烃。产物的分离很容易通过石油醚萃取进行，Pd(PPh3)4/PEG-400 系统可以很容易地回收和重复使用五次，而没有任何显着的活性损失。
• MCM-41-supported bidentate phosphine palladium(0) complex as an efficient catalyst for the heterogeneous Stille reaction
  作者：Hong Zhao、Yue Wang、Junchao Sha、Shouri Sheng、Mingzhong Cai

  DOI：10.1016/j.tet.2008.05.120

  日期：2008.8

  Stille coupling reaction of organostannanes with organic halides has been developed in the presence of a catalytic amount of MCM-41-supported bidentate phosphine palladium(0) complex (0.5 mol %) in DMF/H2O (9:1) under air atmosphere in high yields. This polymeric palladium catalyst exhibits higher activity than Pd(PPh3)4 and can be reused at least 10 times without any decrease in activity.

  在空气中DMF / H 2 O（9：1）中催化量的MCM-41负载的双齿膦膦钯（0）络合物（0.5 mol％）的存在下，开发了有机锡与有机卤化物的Stille偶联反应。高产的气氛。该聚合钯催化剂显示出比Pd（PPh 3）4更高的活性，并且可以重复使用至少10次而活性没有降低。
• TRICYCLIC INHIBITORS OF FATTY ACID AMIDE HYDROLASE
  申请人：Boger Dale L.

  公开号：US20100216750A1

  公开（公告）日：2010-08-26

  A series of substituted oxazole compounds having an alpha keto side chain at the 2 position and an aromatic, heteroaromatic or heterocycle substituent at the 5 position are disclosed. These compounds exhibit inhibition of fatty acid amid hydrolase and arc useful for treatment of malconditions involving that enzyme.

  本发明揭示了一系列取代的噁唑化合物，其中在2位具有α-酮基侧链，在5位具有芳香、杂芳或杂环取代基。这些化合物表现出脂肪酸酰胺水解酶的抑制作用，并且对于治疗涉及该酶的恶性状况是有用的。
• US8124778B2
  申请人：——

  公开号：US8124778B2

  公开（公告）日：2012-02-28
• Structure−Activity Relationships of α-Ketooxazole Inhibitors of Fatty Acid Amide Hydrolase
  作者：Christophe Hardouin、Michael J. Kelso、F. Anthony Romero、Thomas J. Rayl、Donmienne Leung、Inkyu Hwang、Benjamin F. Cravatt、Dale L. Boger

  DOI：10.1021/jm061414r

  日期：2007.7.1

  A systematic study of the structure-activity relationships of 2b (OL-135), a potent inhibitor of fatty acid amide hydrolase (FAAH), is detailed targeting the C2 acyl side chain. A series of aryl replacements or substituents for the terminal phenyl group provided effective inhibitors (e.g., 5c, aryl = 1- napthyl, K-i = 2.6 nM), with 5hh (aryl = 3-ClPh, K-i = 900 pM) being 5-fold more potent than 2b. Conformationally restricted C2 side chains were examined, and many provided exceptionally potent inhibitors, of which 11j (ethylbiphenyl side chain) was established to be a 750 pM inhibitor. A systematic series of heteroatoms (O, NMe, S), electron-withdrawing groups (SO, SO2), and amides positioned within and hydroxyl substitutions on the linking side chain were investigated, which typically led to a loss in potency. The most tolerant positions provided effective inhibitors (12p, 6-position S, K-i = 3 nM, or 13d, 2-position OH, K-i = 8 nM) comparable in potency to 2b. Proteome-wide screening of selected inhibitors from the systematic series of > 100 candidates prepared revealed that they are selective for FAAH over all other mammalian serine proteases.