(E,E)-8-O-(3-benzoylbenzyl)-3,7-dimethyl-2,6-octadiene-1-ol | 185686-49-1

• 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: (E,E)-8-O-(3-benzoylbenzyl)-3,7-dimethyl-2,6-octadiene-1-ol
• 英文别名: [3-[[(2E,6E)-8-hydroxy-2,6-dimethylocta-2,6-dienoxy]methyl]phenyl]-phenylmethanone
• CAS: 185686-49-1
• 化学式: C₂₄H₂₈O₃
• 分子量: 364.485
• InChiKey: NXIHTVHMPKFOGA-APFDVHGWSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5
• 重原子数：
  27
• 可旋转键数：
  10
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.29
• 拓扑面积：
  46.5
• 氢给体数：
  1
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  (E,E)-8-O-(3-benzoylbenzyl)-3,7-dimethyl-2,6-octadiene-1-ol 在 三苯基膦树脂 、 四溴化碳 作用下， 以 二氯甲烷 为溶剂， 生成 (3-((((2E,6E)-8-bromo-2,6-dimethylocta-2,6-dien-1-yl)oxy)methyl)phenyl)(phenyl)methanone
  参考文献：
  名称：

  Synthesis of high specific activity 35S-labelled N-methanesulfonyl farnesylcysteine and a photoactive analog

  摘要：

  前烯丙基化半胱氨酸类似物模拟前烯丙基化 GTP 结合蛋白（G 蛋白）的前烯丙基化半胱氨酸残基，已被广泛用于研究前烯丙基化 G 蛋白的行为。在这一领域的早期研究中，我们制备了光活性类似物 [35S]4，并证明它能在光解时标记 RhoGDI；这些结果与 GDI 包含异肾上腺素结合位点的观点一致。在此，我们介绍了 N-乙酰法尼基半胱氨酸及其甲酯的[35S]N-甲磺酰基标记类似物（1a 和 2a）的制备过程，以及光活性类似物 3 和 4 的改进合成过程；其比活性达到了 1100 Ci/mmol。未标记的化合物 1a 和 2a 被用作光解反应的竞争者，表明甲磺酰胺基是一种合理的乙酰胺取代基。其他实验表明，光活性酯 [35S]3 可以交联纯化形式和粗细菌提取物中的 GDI。然而，使用酯（[35S]3）获得的交联程度明显低于使用游离酸（[35S]4）观察到的交联程度，尽管酯化形式可能更接近于反映前炔化蛋白质 C 端的结构；使用 GDI-Cdc42 共晶体结构，讨论了这些结果的结构基础。Copyright © 2002 John Wiley & Sons, Ltd. All Rights Reserved.

  DOI：

  10.1002/jlcr.638
• 作为产物：
  描述：

  {3-[(2E,6E)-2,6-Dimethyl-8-(tetrahydro-pyran-2-yloxy)-octa-2,6-dienyloxymethyl]-phenyl}-phenyl-methanone 在 4-甲基苯磺酸吡啶 作用下， 以 乙醇 为溶剂， 生成 (E,E)-8-O-(3-benzoylbenzyl)-3,7-dimethyl-2,6-octadiene-1-ol
  参考文献：
  名称：

  法尼基和香叶基香叶基焦磷酸酯类似物并入苯甲酰基苄基醚：酵母蛋白法尼基转移酶的合成和抑制

  摘要：

  描述了结合了稳定的醚连接二苯甲酮的法呢基焦磷酸的两种光敏类似物（1a和1b）的合成。由香叶醇制备化合物1a和1b，总产率为17％。既1A和1B是相对于酵母蛋白质法尼基转移酶的竞争性抑制剂来法尼基焦磷酸和的K 1个49 45纳米的值纳摩。光解12小时后，1a和1b均使酶失活40％

  DOI：

  10.1016/s0040-4039(96)02066-7

文献信息

• A Photoactivatable Prenylated Cysteine Designed to Study Isoprenoid Recognition
  作者：Tamara A. Kale、Conrad Raab、Nathan Yu、Dennis C. Dean、Mark D. Distefano

  DOI：10.1021/ja0012016

  日期：2001.5.1

  Protein prenylation, involving the alkylation of a specific C-terminal cysteine with a C-15 or C-20 isoprenoid unit, is an essential posttranslational modification required by most GTP-binding proteins for normal biological activity. Despite the ubiquitous nature of this modification and numerous efforts aimed at inhibiting prenylating enzymes for therapeutic purposes, the function of prenylation remains unclear. To explore the role the isoprenoid plays in mediating protein-protein recognition, we have synthesized a photoactivatable, isoprenoid-containing cysteine analogue (2) designed to act as a mimic of the C-terminus of prenylated proteins. Photolysis experiments with 2 and RhoCDI (GDI), a protein which interacts with prenylated Rho proteins, suggest that the GDI is in direct contact with the isoprenoid moiety. These results, obtained using purified GDI as well as Escherichia coli (E. coli) crude extract containing GDI, suggest that this analogue will be an effective and versatile tool for the investigation of putative isoprenoid binding sites in a variety of systems. Incorporation of this analogue into peptides or proteins should allow for even more specific interactions between the photoactivatable isoprenoid and any number of isoprenoid binding proteins.
• Farnesyl and geranylgeranyl pyrophosphate analogs incorporating benzoylbenzyl ethers: Synthesis and inhibition of yeast protein farnesyltransferase
  作者：Igor Gaon、Tammy C. Turek、Mark D. Distefano

  DOI：10.1016/s0040-4039(96)02066-7

  日期：1996.12

  The syntheses of two photoactive analogs (1a and 1b) of farnesyl pyrophosphate that incorporate stable ether-linked benzophenones are described. Compounds 1a and 1b were prepared from geraniol in 17% overall yield. Both 1a and 1b are competitive inhibitors of yeast protein famesyltransferase with respect to farnesyl pyrophosphate and have K1 values of 45 nM and 49 nM. Upon photolysis for twelve hours

  描述了结合了稳定的醚连接二苯甲酮的法呢基焦磷酸的两种光敏类似物（1a和1b）的合成。由香叶醇制备化合物1a和1b，总产率为17％。既1A和1B是相对于酵母蛋白质法尼基转移酶的竞争性抑制剂来法尼基焦磷酸和的K 1个49 45纳米的值纳摩。光解12小时后，1a和1b均使酶失活40％
• Synthesis of high specific activity 35S-labelled N-methanesulfonyl farnesylcysteine and a photoactive analog
  作者：Tamara A. Kale、Conrad Raab、Nathan Yu、Evelyn Aquino、Dennis C. Dean、Mark D. Distefano

  DOI：10.1002/jlcr.638

  日期：2003.1

  Prenylated cysteine analogs, which mimic the prenylated cysteine residue of prenylated GTP-binding proteins (G-proteins), have been used in a variety of contexts for the study of prenylated G-protein behavior. In earlier work in this area, we prepared the photoactive analog [35S]4 and showed that it labelled RhoGDI upon photolysis; those results were consistent with the idea that GDI contains an isoprenoid binding site. Here, we describe the preparation of [35S]N-methanesulfonyl labelled analogs (1a and 2a) of N-acetyl farnesylcysteine and its methyl ester together with an improved synthetic procedure for photoactive analogs 3 and 4; specific activities of ∼1100 Ci/mmol were achieved. Compounds 1a and 2a in unlabelled form were used as competitors in photolysis reactions to show that the methanesulfonamido group is a reasonable acetamide substitution. Additional experiments show that the photoactive ester [35S]3 can cross-link GDI in both purified form and crude bacterial extract. However, the extent of cross-linking obtained with the ester ([35S]3) is significantly less than that observed with the free acid ([35S]4) despite the fact that the esterified form probably more closely reflects the structure of the C-terminus of a prenylated protein; using the GDI·Cdc42 co-crystal structure, the structural basis for these results is discussed. Copyright © 2002 John Wiley & Sons, Ltd.

  前烯丙基化半胱氨酸类似物模拟前烯丙基化 GTP 结合蛋白（G 蛋白）的前烯丙基化半胱氨酸残基，已被广泛用于研究前烯丙基化 G 蛋白的行为。在这一领域的早期研究中，我们制备了光活性类似物 [35S]4，并证明它能在光解时标记 RhoGDI；这些结果与 GDI 包含异肾上腺素结合位点的观点一致。在此，我们介绍了 N-乙酰法尼基半胱氨酸及其甲酯的[35S]N-甲磺酰基标记类似物（1a 和 2a）的制备过程，以及光活性类似物 3 和 4 的改进合成过程；其比活性达到了 1100 Ci/mmol。未标记的化合物 1a 和 2a 被用作光解反应的竞争者，表明甲磺酰胺基是一种合理的乙酰胺取代基。其他实验表明，光活性酯 [35S]3 可以交联纯化形式和粗细菌提取物中的 GDI。然而，使用酯（[35S]3）获得的交联程度明显低于使用游离酸（[35S]4）观察到的交联程度，尽管酯化形式可能更接近于反映前炔化蛋白质 C 端的结构；使用 GDI-Cdc42 共晶体结构，讨论了这些结果的结构基础。Copyright © 2002 John Wiley & Sons, Ltd. All Rights Reserved.