L-dehydroascorbic acid 6-palmitate | 63247-05-2

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 脂肪酰基
• 英文名称: L-dehydroascorbic acid 6-palmitate
• 英文别名: Dehydroascorbic acid 6-palmitate；[(2S)-2-hydroxy-2-[(2R)-3,4,5-trioxooxolan-2-yl]ethyl] hexadecanoate
• CAS: 63247-05-2
• 化学式: C₂₂H₃₆O₇
• 分子量: 412.524
• InChiKey: PRDZMCIHNHYBJQ-LAUBAEHRSA-N

物化性质

• 沸点：
  532.6±46.0 °C(Predicted)
• 密度：
  1.115±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  6.9
• 重原子数：
  29
• 可旋转键数：
  18
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.82
• 拓扑面积：
  107
• 氢给体数：
  1
• 氢受体数：
  7

反应信息

• 作为产物：
  描述：

  L-抗坏血酸棕榈酸酯 在 碘 、 碳酸氢钠 作用下， 以 乙醇 为溶剂， 反应 0.5h， 生成 L-dehydroascorbic acid 6-palmitate
  参考文献：
  名称：

  Inactivation of Protein Farnesyltransferase by Active-Site-Targeted Dicarbonyl Compounds

  摘要：

  Upon farnesylation by protein farnesyltransferase (FTase), key proteins become compartmentalized in cells. For example, cell membrane localization is essential for the mitogenic role of mutant Ras protein, which acts as a switch for cancer cell proliferation. We repel? that alpha -dicarbonyl compounds derived from the isoprenoid skeleton or other hydrophobic groups potently obstruct farnesylation of a Ras model peptide by human recombinant FTase in vitro. A geranyl-derived isoprenoid diketone, 5.9-dimethyl-8-decene-2,3-dione, at 17 muM caused a 62% reduction in FTase activity after 30 minutes. A farnesyl-derived isoprenoid diketone, 5,9,13-trimethyl-8,12-tetradecadiene-2,3-dione, at 93 muM caused a 94% reduction after 30 minutes. Other dicarbonyl:compounds found to be effective against FTase in vitro were (+/-)-6-(camphorquinone-10-sulfonamido)-hexanoic acid, 4,4 ' -biphenyldiglyoxaldehyde, dehydroascorbic acid 6-palmitace, 2-oxododecanal, and phenylglyoxal. Higher concentrations of the alpha -dicarbonyl compound resulted in more rapid and more extensive inactivation. These findings demonstrate that ct-dicarbonyl compounds targeted to FTase interfere with protein farnesylation in vitro and may,lead to derivatives that have utility as chemotherapeutic agents.

  DOI：

  10.1002/1521-4184(200106)334:6<194::aid-ardp194>3.0.co;2-m

文献信息

• Compositions comprising Quinone and/or Quinol and methods of preparations and use thereof
  申请人：American River Nutrition, LLC

  公开号：US20210113491A1

  公开（公告）日：2021-04-22

  The present embodiments are directed to compositions of quinones and/or quinols, such as, but not limited to, ubiquinone and/or ubiquinol, vitamin E quinone and/or vitamin E quinol, vitamin K quinone and/or vitamin K quinol, menaquinones and/or menaquinols, and pyrroloquinoline quinone and/or pyrroloquinoline quinol, and methods for preparations and use thereof. The present embodiments are also directed to compositions of reduced forms of curcuminoid and methods for preparations and use thereof.
• Inactivation of Protein Farnesyltransferase by Active-Site-Targeted Dicarbonyl Compounds
  作者：Karl J. Okolotowicz、Wei-Jen Lee、Rosemarie F. Hartman、Ann Y. Kim、Steven R. Ottersberg、Dale E. Robinson, Jr.、Scott R. Lefler、Seth D. Rose

  DOI：10.1002/1521-4184(200106)334:6<194::aid-ardp194>3.0.co;2-m

  日期：2001.6

  Upon farnesylation by protein farnesyltransferase (FTase), key proteins become compartmentalized in cells. For example, cell membrane localization is essential for the mitogenic role of mutant Ras protein, which acts as a switch for cancer cell proliferation. We repel? that alpha -dicarbonyl compounds derived from the isoprenoid skeleton or other hydrophobic groups potently obstruct farnesylation of a Ras model peptide by human recombinant FTase in vitro. A geranyl-derived isoprenoid diketone, 5.9-dimethyl-8-decene-2,3-dione, at 17 muM caused a 62% reduction in FTase activity after 30 minutes. A farnesyl-derived isoprenoid diketone, 5,9,13-trimethyl-8,12-tetradecadiene-2,3-dione, at 93 muM caused a 94% reduction after 30 minutes. Other dicarbonyl:compounds found to be effective against FTase in vitro were (+/-)-6-(camphorquinone-10-sulfonamido)-hexanoic acid, 4,4 ' -biphenyldiglyoxaldehyde, dehydroascorbic acid 6-palmitace, 2-oxododecanal, and phenylglyoxal. Higher concentrations of the alpha -dicarbonyl compound resulted in more rapid and more extensive inactivation. These findings demonstrate that ct-dicarbonyl compounds targeted to FTase interfere with protein farnesylation in vitro and may,lead to derivatives that have utility as chemotherapeutic agents.