dimethyl (E)-6-(hydroxymethyl)undec-4-enedioate | 205592-46-7

• 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: dimethyl (E)-6-(hydroxymethyl)undec-4-enedioate
• CAS: 205592-46-7
• 化学式: C₁₄H₂₄O₅
• 分子量: 272.342
• InChiKey: YPLWANSANWBDBV-XVNBXDOJSA-N

物化性质

• 沸点：
  358.9±42.0 °C(Predicted)
• 密度：
  1.055±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  1.5
• 重原子数：
  19
• 可旋转键数：
  12
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.71
• 拓扑面积：
  72.8
• 氢给体数：
  1
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  dimethyl (E)-6-(hydroxymethyl)undec-4-enedioate 在 氢氧化钾 、 偶氮二甲酸二异丙酯 、 三苯基膦 作用下， 以 四氢呋喃 、 乙醇 为溶剂， 反应 5.0h， 生成 (E)-6-(sulfanylmethyl)undec-4-enedioic acid
  参考文献：
  名称：

  Synthesis and Glutathione S-Transferase Structure−Affinity Relationships of Nonpeptide and Peptidase-Stable Glutathione Analogues

  摘要：

  A series of nonpeptidic glutathione analogues where the peptide bonds were replaced by simple carbon-carbon bonds or isosteric E double bonds were prepared. The optimal length for the two alkyl chains on either side of the mercaptomethyl group was evaluated using structure-affinity relationships. Affinities of the analogues 14a-f, 23, and 25 were evaluated for a recombinant GST enzyme using a new affinity chromatography method previously developed in our laboratory. Analysis of these analogues gives an additional understanding for GST affinity requirements: (a) the carbon skeleton must conserve that of glutathione since analogue 14a showed the best affinity (IC50 = 5.2 mu M); (b) the GST G site is not able to accommodate a chain length elongation of one methylene group (no affinity for analogues 14c,f); (c) a one-methylene group chain length reduction is tolerated, much more for the "Glu side" (14d, IC50 = 10.1 mu M) than for the "Gly side" (14b, IC50 = 1800 mu M); (d) the mercaptomethyl group must remain at position 5 as shown from the null affinity of the 6-mercaptomethyl analogue 14e; (e) the additional, peptide isosteric E double bond (25) or hydroxyl derivative (23) in 14e did not help to retrieve affinity, This work reveals useful. information for the design of new selective nonpeptidic and peptidase-stable glutathione analogues.

  DOI：

  10.1021/jm970518m
• 作为产物：
  描述：

  6-oxo-undecanedioic acid dimethyl ester 在 sodium hydroxide 、 9-borabicyclo[3.3.1]nonane dimer 、 水 、 双氧水 、 溴 、 silica gel 、 对甲苯磺酸 、 1,8-二氮杂双环[5.4.0]十一碳-7-烯 、 三氟乙酸 作用下， 以 四氢呋喃 、 乙醚 、 正己烷 、 二氯甲烷 、 二甲基亚砜 、 苯 为溶剂， 反应 16.17h， 生成 dimethyl (E)-6-(hydroxymethyl)undec-4-enedioate
  参考文献：
  名称：

  Synthesis and Glutathione S-Transferase Structure−Affinity Relationships of Nonpeptide and Peptidase-Stable Glutathione Analogues

  摘要：

  A series of nonpeptidic glutathione analogues where the peptide bonds were replaced by simple carbon-carbon bonds or isosteric E double bonds were prepared. The optimal length for the two alkyl chains on either side of the mercaptomethyl group was evaluated using structure-affinity relationships. Affinities of the analogues 14a-f, 23, and 25 were evaluated for a recombinant GST enzyme using a new affinity chromatography method previously developed in our laboratory. Analysis of these analogues gives an additional understanding for GST affinity requirements: (a) the carbon skeleton must conserve that of glutathione since analogue 14a showed the best affinity (IC50 = 5.2 mu M); (b) the GST G site is not able to accommodate a chain length elongation of one methylene group (no affinity for analogues 14c,f); (c) a one-methylene group chain length reduction is tolerated, much more for the "Glu side" (14d, IC50 = 10.1 mu M) than for the "Gly side" (14b, IC50 = 1800 mu M); (d) the mercaptomethyl group must remain at position 5 as shown from the null affinity of the 6-mercaptomethyl analogue 14e; (e) the additional, peptide isosteric E double bond (25) or hydroxyl derivative (23) in 14e did not help to retrieve affinity, This work reveals useful. information for the design of new selective nonpeptidic and peptidase-stable glutathione analogues.

  DOI：

  10.1021/jm970518m

文献信息

• Synthesis and Glutathione <i>S</i>-Transferase Structure−Affinity Relationships of Nonpeptide and Peptidase-Stable Glutathione Analogues
  作者：Philippe Klotz、Amal Slaoui-Hasnaoui、Jean-Louis Banères、Jean-Frédéric Duckert、Jean-Claude Rossi、Abdelali Kerbal

  DOI：10.1021/jm970518m

  日期：1998.6.1

  A series of nonpeptidic glutathione analogues where the peptide bonds were replaced by simple carbon-carbon bonds or isosteric E double bonds were prepared. The optimal length for the two alkyl chains on either side of the mercaptomethyl group was evaluated using structure-affinity relationships. Affinities of the analogues 14a-f, 23, and 25 were evaluated for a recombinant GST enzyme using a new affinity chromatography method previously developed in our laboratory. Analysis of these analogues gives an additional understanding for GST affinity requirements: (a) the carbon skeleton must conserve that of glutathione since analogue 14a showed the best affinity (IC50 = 5.2 mu M); (b) the GST G site is not able to accommodate a chain length elongation of one methylene group (no affinity for analogues 14c,f); (c) a one-methylene group chain length reduction is tolerated, much more for the "Glu side" (14d, IC50 = 10.1 mu M) than for the "Gly side" (14b, IC50 = 1800 mu M); (d) the mercaptomethyl group must remain at position 5 as shown from the null affinity of the 6-mercaptomethyl analogue 14e; (e) the additional, peptide isosteric E double bond (25) or hydroxyl derivative (23) in 14e did not help to retrieve affinity, This work reveals useful. information for the design of new selective nonpeptidic and peptidase-stable glutathione analogues.