(+/-)-6-(camphor-10-sulfonamido)-hexanoic acid

• 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: (+/-)-6-(camphor-10-sulfonamido)-hexanoic acid
• 英文别名: 6-[[(1S,4R)-7,7-dimethyl-2-oxo-1-bicyclo[2.2.1]heptanyl]methylsulfonylamino]hexanoic acid
• 化学式: C₁₆H₂₇NO₅S
• 分子量: 345.46
• InChiKey: RMGLEMNTOUMUJU-MLGOLLRUSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.3
• 重原子数：
  23
• 可旋转键数：
  9
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.88
• 拓扑面积：
  109
• 氢给体数：
  2
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  (+/-)-6-(camphor-10-sulfonamido)-hexanoic acid 在 selenium(IV) oxide 作用下， 以 1,4-二氧六环 、 水 为溶剂， 反应 120.0h， 生成 (+/-)-6-(camphorquinone-10-sulfonamido)-hexanoic acid
  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
• 作为产物：
  描述：

  D(+)-10-樟脑磺酸 在 氯化亚砜 、 magnesium oxide 作用下， 以 1,4-二氧六环 、 水 、 N,N-二甲基甲酰胺 为溶剂， 反应 20.75h， 生成 (+/-)-6-(camphor-10-sulfonamido)-hexanoic acid
  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

• 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.