(2E,4Z,6Z,8E)-6-Fluoro-3,7-dimethyl-9-(2,6,6-trimethyl-cyclohex-1-enyl)-nona-2,4,6,8-tetraenal | 68200-16-8

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 异戊烯醇脂质
• 英文名称: (2E,4Z,6Z,8E)-6-Fluoro-3,7-dimethyl-9-(2,6,6-trimethyl-cyclohex-1-enyl)-nona-2,4,6,8-tetraenal
• 英文别名: (2E,4Z,6Z,8E)-6-fluoro-3,7-dimethyl-9-(2,6,6-trimethylcyclohexen-1-yl)nona-2,4,6,8-tetraenal
• CAS: 68200-16-8
• 化学式: C₂₀H₂₇FO
• 分子量: 302.432
• InChiKey: LWQLDNOODFVDOM-WBUSAKPRSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5.8
• 重原子数：
  22
• 可旋转键数：
  5
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.45
• 拓扑面积：
  17.1
• 氢给体数：
  0
• 氢受体数：
  2

反应信息

• 作为反应物：
  描述：

  (2E,4Z,6Z,8E)-6-Fluoro-3,7-dimethyl-9-(2,6,6-trimethyl-cyclohex-1-enyl)-nona-2,4,6,8-tetraenal 以 正己烷 、 氯仿 为溶剂， 生成 Butyl-[(2E,4E,6E,8E)-4-fluoro-3,7-dimethyl-9-(2,6,6-trimethyl-cyclohex-1-enyl)-nona-2,4,6,8-tetraen-(Z)-ylidene]-amine; compound with trichloro-acetic acid
  参考文献：
  名称：

  A ¹⁹F NMR Study of Rhodopsin Analogs:  Use of Vinylfluororetinal Chromophores

  摘要：

  F-19 NMR spectra of 11-cis and 9-cis isomers of six fluorinated rhodopsin analogs with the label(s) located at the vinylic positions of the polyene chain (8-F, 10-F, 12-F, 14-F, 8,12-F-2, 10,14-F-2) are reported along with their UV-vis and CD spectra. The regiospecific F chemical shift data are analyzed in terms of chromophore changes and local perturbation resulting from specific interactions with protein. Two analogs (11-cis-12-F and 11-cis-8-F) and also 9,11-di-cis-12-F possess FOS (fluorine opsin shift) values uniquely different from others. Ab initio F NMR chemical shielding calculations of model structures provide support that a strong protein perturbation to the 12-F position prevails in the binding cavity and that F-8 shift is sensitive to variation of the nearby dihedral angle(s). Possible causes for the broad line width of the F signals of these membrane proteins are discussed.

  DOI：

  10.1021/jp952850k
• 作为产物：
  描述：

  (7E,9Z,11E,13E)-10-fluoro-retinal 以 乙腈 为溶剂， 生成 (2E,4Z,6Z,8E)-6-Fluoro-3,7-dimethyl-9-(2,6,6-trimethyl-cyclohex-1-enyl)-nona-2,4,6,8-tetraenal
  参考文献：
  名称：

  Fluoro Derivatives of Retinal Illuminate the Decisive Role of the C₁₂-H Element in Photoisomerization and Rhodopsin Activation

  摘要：

  Rhodopsin, the visual pigment of the vertebrate rod cell, is among the best investigated members of the G-protein-coupled receptor family. Within this family a unique characteristic of visual pigments is their covalently bound chromophore, 11-cis retinal, which acts as an inverse agonist. Upon illumination it can be transformed into the all-trans isomer that acts as a full agonist. This photoisomerization process is extremely efficient: 2 out of 3 photons are effective, full stereoselectivity is achieved, and stereoinversion occurs within 200 fs. The mechanism behind this process is still not really understood, although the available evidence points at the twisted C-9-C-13 segment of the 11-cis ligand as the quintessence. To further dissect the role of this segment, we have generated the 10-fluoro, 12-fluoro, and 14-fluoro analogues of rhodopsin. A fluoro substituent brings in only little more volume than hydrogen, but considerably more mass and polarizability. The analogue pigments were compared to rhodopsin with respect to their photosensitivity (quantum yield), light-induced structural transitions (UV-vis and FT-IR spectroscopy), and signaling activity (G protein activation rate). We find that 14-F substitution is quite neutral, while 10-F and 12-F substitutions exert significant but distinct effects. The 10-F pigment exhibits a quantum yield similar to that of rhodopsin (0.65) but strongly perturbed thermodynamics of the structural transitions following photoactivation and only 20% of the native signaling activity. The 12-F pigment exhibits a significantly decreased quantum yield (0.47) and signaling activity (30%) but mixed effects on the structural transitions. These properties are compared to those of the corresponding methyl derivatives. We conclude that rotation of the C-12-H bond of the rhodopsin chromophore is a major rate-limiting factor in the photoisomerization process, while the C-10-H moiety plays a dominant role in ligand relaxation and further rearrangements following photoactivation.

  DOI：

  10.1021/ja907577p

文献信息

• A ¹⁹F NMR Study of Rhodopsin Analogs:  Use of Vinylfluororetinal Chromophores
  作者：Leticia U. Colmenares、Walter P. Niemczura、Alfred E. Asato、Robert S. H. Liu

  DOI：10.1021/jp952850k

  日期：1996.1.1

  F-19 NMR spectra of 11-cis and 9-cis isomers of six fluorinated rhodopsin analogs with the label(s) located at the vinylic positions of the polyene chain (8-F, 10-F, 12-F, 14-F, 8,12-F-2, 10,14-F-2) are reported along with their UV-vis and CD spectra. The regiospecific F chemical shift data are analyzed in terms of chromophore changes and local perturbation resulting from specific interactions with protein. Two analogs (11-cis-12-F and 11-cis-8-F) and also 9,11-di-cis-12-F possess FOS (fluorine opsin shift) values uniquely different from others. Ab initio F NMR chemical shielding calculations of model structures provide support that a strong protein perturbation to the 12-F position prevails in the binding cavity and that F-8 shift is sensitive to variation of the nearby dihedral angle(s). Possible causes for the broad line width of the F signals of these membrane proteins are discussed.
• Fluoro Derivatives of Retinal Illuminate the Decisive Role of the C₁₂-H Element in Photoisomerization and Rhodopsin Activation
  作者：Petra H. M. Bovee-Geurts、Isabelle Fernández Fernández、Robert S. H. Liu、Richard A. Mathies、Johan Lugtenburg、Willem J. DeGrip

  DOI：10.1021/ja907577p

  日期：2009.12.16

  Rhodopsin, the visual pigment of the vertebrate rod cell, is among the best investigated members of the G-protein-coupled receptor family. Within this family a unique characteristic of visual pigments is their covalently bound chromophore, 11-cis retinal, which acts as an inverse agonist. Upon illumination it can be transformed into the all-trans isomer that acts as a full agonist. This photoisomerization process is extremely efficient: 2 out of 3 photons are effective, full stereoselectivity is achieved, and stereoinversion occurs within 200 fs. The mechanism behind this process is still not really understood, although the available evidence points at the twisted C-9-C-13 segment of the 11-cis ligand as the quintessence. To further dissect the role of this segment, we have generated the 10-fluoro, 12-fluoro, and 14-fluoro analogues of rhodopsin. A fluoro substituent brings in only little more volume than hydrogen, but considerably more mass and polarizability. The analogue pigments were compared to rhodopsin with respect to their photosensitivity (quantum yield), light-induced structural transitions (UV-vis and FT-IR spectroscopy), and signaling activity (G protein activation rate). We find that 14-F substitution is quite neutral, while 10-F and 12-F substitutions exert significant but distinct effects. The 10-F pigment exhibits a quantum yield similar to that of rhodopsin (0.65) but strongly perturbed thermodynamics of the structural transitions following photoactivation and only 20% of the native signaling activity. The 12-F pigment exhibits a significantly decreased quantum yield (0.47) and signaling activity (30%) but mixed effects on the structural transitions. These properties are compared to those of the corresponding methyl derivatives. We conclude that rotation of the C-12-H bond of the rhodopsin chromophore is a major rate-limiting factor in the photoisomerization process, while the C-10-H moiety plays a dominant role in ligand relaxation and further rearrangements following photoactivation.