N-tert-butoxycarbonyl O-[2-acetamido-4,6-di-O-acetyl-2-deoxy-3-O-(2,3,4,6-tetra-O-acetyl-α-D-galactopyranosyl)-α-D-galactopyranosyl]-L-threonine tert-butylester | 875484-85-8

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: N-tert-butoxycarbonyl O-[2-acetamido-4,6-di-O-acetyl-2-deoxy-3-O-(2,3,4,6-tetra-O-acetyl-α-D-galactopyranosyl)-α-D-galactopyranosyl]-L-threonine tert-butylester
• CAS: 875484-85-8
• 化学式: C₃₉H₆₀N₂O₂₁
• 分子量: 892.906
• InChiKey: DUNHCQXZJRREDR-GMXXJWBSSA-N

反应信息

• 作为反应物：
  描述：

  N-tert-butoxycarbonyl O-[2-acetamido-4,6-di-O-acetyl-2-deoxy-3-O-(2,3,4,6-tetra-O-acetyl-α-D-galactopyranosyl)-α-D-galactopyranosyl]-L-threonine tert-butylester 在 三氟乙酸 作用下， 以 二氯甲烷 为溶剂， 反应 24.0h， 生成 (2S,3R)-3-[(2S,3R,4R,5R,6R)-5-Acetoxy-6-acetoxymethyl-3-acetylamino-4-((2S,3R,4S,5S,6R)-3,4,5-triacetoxy-6-acetoxymethyl-tetrahydro-pyran-2-yloxy)-tetrahydro-pyran-2-yloxy]-2-amino-butyric acid
  参考文献：
  名称：

  Chemical synthesis of analogs of the glycopeptide contulakin-G, an analgetically active conopeptide from Conus geographus

  摘要：

  Cone snails are marine predators that use immobilizing venoms for catching prey. Chemical analysis of the venoms has revealed a variety of biologically active small and intermediate size peptides rich in post-translational modifications (modified amino acids, glycosylation). The glycopeptide contulakin-G(pGlu-Ser-Glu-Glu-Gly-Gly-Ser-Asn-Ala-[beta-D-Galp-(1 -> 3)-alpha-D-GalpNAc(I ->]Thr-Lys-Lys-Pro-Tyr-Ile-Leu-OH) is a potent analgesic from Conus geographus venom. The in vivo activity of synthetic contulakin-G was previously found to be significantly higher compared to that of a peptide lacking the glycan. In order to further investigate the importance of the glycan, we have now synthesized analogs of contulakin-G where the glycan chain O-linked to threonine has been altered either to beta-D-Galp-(1 -> 3)-P-D-GalpNAc-, alpha-D-Galp-(1 -> 3)-alpha-D-GalpNAc-, or beta-D-Galp-(1 -> 6)-alpha-D-GalP-NAc-. The glycopeptides were assembled on a Wang resin using commercially available Fmoc amino acids and synthetically prepared Fmoc-protected threonine derivatives carrying O-acetyl protected sugar chains. The final products were thoroughly characterized by NMR and mass spectroscopy. (c) 2005 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.carres.2005.11.010
• 作为产物：
  描述：

  (2S,3R)-3-[(2S,3R,4R,5R,6R)-3-Amino-5-hydroxy-6-hydroxymethyl-4-((2S,3R,4S,5R,6R)-3,4,5-trihydroxy-6-hydroxymethyl-tetrahydro-pyran-2-yloxy)-tetrahydro-pyran-2-yloxy]-2-tert-butoxycarbonylamino-butyric acid tert-butyl ester 、 乙酸酐 以 吡啶 为溶剂， 反应 24.0h， 以635 mg的产率得到N-tert-butoxycarbonyl O-[2-acetamido-4,6-di-O-acetyl-2-deoxy-3-O-(2,3,4,6-tetra-O-acetyl-α-D-galactopyranosyl)-α-D-galactopyranosyl]-L-threonine tert-butylester
  参考文献：
  名称：

  Chemical synthesis of analogs of the glycopeptide contulakin-G, an analgetically active conopeptide from Conus geographus

  摘要：

  Cone snails are marine predators that use immobilizing venoms for catching prey. Chemical analysis of the venoms has revealed a variety of biologically active small and intermediate size peptides rich in post-translational modifications (modified amino acids, glycosylation). The glycopeptide contulakin-G(pGlu-Ser-Glu-Glu-Gly-Gly-Ser-Asn-Ala-[beta-D-Galp-(1 -> 3)-alpha-D-GalpNAc(I ->]Thr-Lys-Lys-Pro-Tyr-Ile-Leu-OH) is a potent analgesic from Conus geographus venom. The in vivo activity of synthetic contulakin-G was previously found to be significantly higher compared to that of a peptide lacking the glycan. In order to further investigate the importance of the glycan, we have now synthesized analogs of contulakin-G where the glycan chain O-linked to threonine has been altered either to beta-D-Galp-(1 -> 3)-P-D-GalpNAc-, alpha-D-Galp-(1 -> 3)-alpha-D-GalpNAc-, or beta-D-Galp-(1 -> 6)-alpha-D-GalP-NAc-. The glycopeptides were assembled on a Wang resin using commercially available Fmoc amino acids and synthetically prepared Fmoc-protected threonine derivatives carrying O-acetyl protected sugar chains. The final products were thoroughly characterized by NMR and mass spectroscopy. (c) 2005 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.carres.2005.11.010