3-O-(6-O-α-D-galactopyranosyl-β-D-galactopyranosyl)-1,2-di-O-dodecanoyl-sn-glycerol

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 甘油脂
• 英文名称: 3-O-(6-O-α-D-galactopyranosyl-β-D-galactopyranosyl)-1,2-di-O-dodecanoyl-sn-glycerol
• 英文别名: 3-[alpha-D-galactosyl-(1->6)-beta-D-galactosyl]-1,2-didodecanoyl-sn-glycerol；[(2S)-2-dodecanoyloxy-3-[(2R,3R,4S,5R,6R)-3,4,5-trihydroxy-6-[[(2S,3R,4S,5R,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxymethyl]oxan-2-yl]oxypropyl] dodecanoate
• 化学式: C₃₉H₇₂O₁₅
• 分子量: 780.992
• InChiKey: FYXYTEZUINAIJQ-TWAAJEGHSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  6
• 重原子数：
  54
• 可旋转键数：
  32
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.95
• 拓扑面积：
  231
• 氢给体数：
  7
• 氢受体数：
  15

反应信息

• 作为反应物：
  描述：

  3-O-(6-O-α-D-galactopyranosyl-β-D-galactopyranosyl)-1,2-di-O-dodecanoyl-sn-glycerol 、 水 生成 laurate anion 、 dodecanoyl-3-O-[α-D-galactosyl-(1→6)-β-D-galactosyl]-sn-glycerol 、 氢(+1)阳离子
  参考文献：
  名称：

  在酵母细胞中表达的人类胰腺脂肪酶相关蛋白2的进一步生化特征。

  摘要：

  重组人胰腺脂肪酶相关蛋白2（rHPLRP2）在蛋白酶A缺陷型酵母毕赤酵母中产生。使用SP-琼脂糖和Mono Q色谱从培养基中纯化出分子量为50kDa的主要蛋白质。发现该蛋白质对在盖结构域中的肽键的蛋白水解切割高度敏感。盖子中发生的蛋白水解切割过程影响了rHPLRP2的脂肪酶和磷脂酶活性。使用pH调节剂和单分子膜技术以及各种底物（甘油酯，磷脂和半乳糖脂）研究了非蛋白水解rHPLRP2的底物特异性。所有酶的活性在碱性pH值时最大，在pH 5-7范围内降低，这与十二指肠中发生的生理条件相对应。发现rHPLRP2优先作用于在溶液中形成小聚集体的基质（甘油单酯，卵磷脂酰胆碱和半乳糖脂），而不是乳化的基质（如三油精和二油精）。测定了rHPLRP2对单半乳糖基甘油二酸酯和二半乳糖基甘油二酸酯单分子膜的活性，并将其与豚鼠胰腺脂肪酶相关蛋白2的活性进行了比较，后者在盖结构域中显示出大的缺失。rHPLRP2中

  DOI：

  10.1194/jlr.m600486-jlr200
• 作为产物：
  描述：

  3-O-[6-O-(2,3,4,6-tetra-O-benzyl-α-D-galactopyranosyl)-2,3,4-tri-O-benzyl-β-D-galactopyranosyl]-1,2-di-O-dodecanoyl-sn-glycerol 在 palladium dihydroxide 环己烯 作用下， 以 乙醇 为溶剂， 反应 5.0h， 以75%的产率得到3-O-(6-O-α-D-galactopyranosyl-β-D-galactopyranosyl)-1,2-di-O-dodecanoyl-sn-glycerol
  参考文献：
  名称：

  Syntheses of an α-d-Gal-(1→6)-β-d-Gal diglyceride, as lipase substrate

  摘要：

  Two different routes were explored to afford 3-O-(6-0-alpha-D-galactopyranosyl-beta-D-galactopyranosyl)-1,2-di-O-dodecanoyl-sn-glycerol. In the first one, the key step was the glycosylation of the 3-O-(2,3,4-tri-O-benzyl-beta-D-galactopyranosyl)- 1, 2-O-isopropylidene-sn-glycerol acceptor with 2-pyridyl 2,3,4,6-tetra-O-benzyl-1-thio-beta-D-galactopyranoside as the donor. In the second one, the key step was the coupling of 2,3,4-tri-O-acetyl-6-O-(2,3,4,6-tetra-O-benzyl-alpha-D-galactopyranosyl)-D-galactopyranosyl trichloroacetimidate donor with 1,2-O-isopropylidene-sn-glycerol. Even though the number of steps was the same in both pathways, the first one afforded a better overall yield (12.4%) than the second one (6.5%). This eight-step synthesis allowed the preparation of the expected glycolipid, which was used as substrate for recombinant GPLRP2 galactolipase using the monomolecular film technique. (c) 2006 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.carres.2006.01.021

文献信息

• Syntheses of an α-d-Gal-(1→6)-β-d-Gal diglyceride, as lipase substrate
  作者：Dominique Lafont、Frédéric Carrière、Francine Ferrato、Paul Boullanger

  DOI：10.1016/j.carres.2006.01.021

  日期：2006.5

  Two different routes were explored to afford 3-O-(6-0-alpha-D-galactopyranosyl-beta-D-galactopyranosyl)-1,2-di-O-dodecanoyl-sn-glycerol. In the first one, the key step was the glycosylation of the 3-O-(2,3,4-tri-O-benzyl-beta-D-galactopyranosyl)- 1, 2-O-isopropylidene-sn-glycerol acceptor with 2-pyridyl 2,3,4,6-tetra-O-benzyl-1-thio-beta-D-galactopyranoside as the donor. In the second one, the key step was the coupling of 2,3,4-tri-O-acetyl-6-O-(2,3,4,6-tetra-O-benzyl-alpha-D-galactopyranosyl)-D-galactopyranosyl trichloroacetimidate donor with 1,2-O-isopropylidene-sn-glycerol. Even though the number of steps was the same in both pathways, the first one afforded a better overall yield (12.4%) than the second one (6.5%). This eight-step synthesis allowed the preparation of the expected glycolipid, which was used as substrate for recombinant GPLRP2 galactolipase using the monomolecular film technique. (c) 2006 Elsevier Ltd. All rights reserved.
• Further biochemical characterization of human pancreatic lipase-related protein 2 expressed in yeast cells
  作者：Cécilia Eydoux、Josiane De Caro、Francine Ferrato、Paul Boullanger、Dominique Lafont、René Laugier、Frédéric Carrière、Alain De Caro

  DOI：10.1194/jlr.m600486-jlr200

  日期：2007.7

  with a molecular mass of 50 kDa was purified from the culture medium using SP-Sepharose and Mono Q chromatography. The protein was found to be highly sensitive to the proteolytic cleavage of a peptide bond in the lid domain. The proteolytic cleavage process occurring in the lid affected both the lipase and phospholipase activities of rHPLRP2. The substrate specificity of the nonproteolyzed rHPLRP2 was

  重组人胰腺脂肪酶相关蛋白2（rHPLRP2）在蛋白酶A缺陷型酵母毕赤酵母中产生。使用SP-琼脂糖和Mono Q色谱从培养基中纯化出分子量为50kDa的主要蛋白质。发现该蛋白质对在盖结构域中的肽键的蛋白水解切割高度敏感。盖子中发生的蛋白水解切割过程影响了rHPLRP2的脂肪酶和磷脂酶活性。使用pH调节剂和单分子膜技术以及各种底物（甘油酯，磷脂和半乳糖脂）研究了非蛋白水解rHPLRP2的底物特异性。所有酶的活性在碱性pH值时最大，在pH 5-7范围内降低，这与十二指肠中发生的生理条件相对应。发现rHPLRP2优先作用于在溶液中形成小聚集体的基质（甘油单酯，卵磷脂酰胆碱和半乳糖脂），而不是乳化的基质（如三油精和二油精）。测定了rHPLRP2对单半乳糖基甘油二酸酯和二半乳糖基甘油二酸酯单分子膜的活性，并将其与豚鼠胰腺脂肪酶相关蛋白2的活性进行了比较，后者在盖结构域中显示出大的缺失。rHPLRP2中