O-(2-azido-4O,6O-benzylidene-2-deoxy-α-D-galactopyranosyl)-N-[(9H-fluoren-9-yl)-methoxycarbonyl]-(4R)-L-hydroxyproline tert-butyl ester | 1439931-03-9

• 分子结构分类: 有机化合物 - 苯类化合物 - 芴
• 英文名称: O-(2-azido-4O,6O-benzylidene-2-deoxy-α-D-galactopyranosyl)-N-[(9H-fluoren-9-yl)-methoxycarbonyl]-(4R)-L-hydroxyproline tert-butyl ester
• CAS: 1439931-03-9
• 化学式: C₃₇H₄₀N₄O₉
• 分子量: 684.746
• InChiKey: CVJGLTDTPQEVMT-RJPKMPMLSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5.62
• 重原子数：
  50.0
• 可旋转键数：
  7.0
• 环数：
  7.0
• sp3杂化的碳原子比例：
  0.46
• 拓扑面积：
  161.75
• 氢给体数：
  1.0
• 氢受体数：
  10.0

反应信息

• 作为反应物：
  描述：

  O-(2-azido-4O,6O-benzylidene-2-deoxy-α-D-galactopyranosyl)-N-[(9H-fluoren-9-yl)-methoxycarbonyl]-(4R)-L-hydroxyproline tert-butyl ester 在 吡啶 、 4-二甲氨基吡啶 、 水 、 溶剂黄146 作用下， 以 1,2-二氯乙烷 为溶剂， 反应 39.5h， 生成 O-[O-(2',3',4',6'-tetra-O-acetyl-β-D-galactopyranosyl)-[1'→3]-(4,6-di-O-acetyl-2-azido-2-deoxy-α-D-galactopyranosyl)]-N-[(9H-fluoren-9-yl)-methoxycarbonyl]-(4R)-L-hydroxyproline tert-butyl ester
  参考文献：
  名称：

  Synthesis of peptides and glycopeptides with polyproline II helical topology as potential antifreeze molecules

  摘要：

  A library of peptides and glycopeptides containing (4R)-hydroxy-L-proline (Hyp) residues were designed with a view to providing stable polyproline II (PPII) helical molecules with antifreeze activity. A library of dodecapeptides containing contiguous Hyp residues or an Ala-Hyp-Ala tripeptide repeat sequence were synthesized with and without alpha-O-linked N-acetylgalactosamine and a-O-linked galactose-beta-(1 -> 3)-N-acetylgalactosamine appended to the peptide backbone. All (glyco) peptides possessed PPII helical secondary structure with some showing significant thermal stability. The majority of the (glyco) peptides did not exhibit thermal hysteresis (TH) activity and were not capable of modifying the morphology of ice crystals. However, an unglycosylated Ala-Hyp-Ala repeat peptide did show significant TH and ice crystal re-shaping activity suggesting that it was capable of binding to the surface of ice. All (glyco) peptides synthesized displayed some ice recrystallization inhibition (IRI) activity with unglycosylated peptides containing the Ala-Hyp-Ala motif exhibiting the most potent inhibitory activity. Interestingly, although glycosylation is critical to the activity of native antifreeze glycoproteins (AFGPs) that possess an Ala-Thr-Ala tripeptide repeat, this same structural modification is detrimental to the antifreeze activity of the Ala-Hyp-Ala repeat peptides studied here. (C) 2013 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2013.02.025
• 作为产物：
  描述：

  O-(3,4,6-tri-O-acetyl-2-azido-2-deoxy-D-galactopyranosyl)-N-[(9H-fluoren-9-yl)-methoxycarbonyl]-trans-L-hydroxyproline tert-butyl ester 在 sodium methylate 、 对甲苯磺酸 作用下， 以 甲醇 、 N,N-二甲基甲酰胺 为溶剂， 20.0~50.0 ℃ 、12.0 kPa 条件下， 反应 21.0h， 生成 O-(2-azido-4O,6O-benzylidene-2-deoxy-α-D-galactopyranosyl)-N-[(9H-fluoren-9-yl)-methoxycarbonyl]-(4R)-L-hydroxyproline tert-butyl ester 、 O-(2-azido-4O,6O-benzylidene-2-deoxy-β-D-galactopyranosyl)-N-[(9H-fluoren-9-yl)-methoxycarbonyl]-(4R)-L-hydroxyproline tert-butyl ester
  参考文献：
  名称：

  Synthesis of peptides and glycopeptides with polyproline II helical topology as potential antifreeze molecules

  摘要：

  A library of peptides and glycopeptides containing (4R)-hydroxy-L-proline (Hyp) residues were designed with a view to providing stable polyproline II (PPII) helical molecules with antifreeze activity. A library of dodecapeptides containing contiguous Hyp residues or an Ala-Hyp-Ala tripeptide repeat sequence were synthesized with and without alpha-O-linked N-acetylgalactosamine and a-O-linked galactose-beta-(1 -> 3)-N-acetylgalactosamine appended to the peptide backbone. All (glyco) peptides possessed PPII helical secondary structure with some showing significant thermal stability. The majority of the (glyco) peptides did not exhibit thermal hysteresis (TH) activity and were not capable of modifying the morphology of ice crystals. However, an unglycosylated Ala-Hyp-Ala repeat peptide did show significant TH and ice crystal re-shaping activity suggesting that it was capable of binding to the surface of ice. All (glyco) peptides synthesized displayed some ice recrystallization inhibition (IRI) activity with unglycosylated peptides containing the Ala-Hyp-Ala motif exhibiting the most potent inhibitory activity. Interestingly, although glycosylation is critical to the activity of native antifreeze glycoproteins (AFGPs) that possess an Ala-Thr-Ala tripeptide repeat, this same structural modification is detrimental to the antifreeze activity of the Ala-Hyp-Ala repeat peptides studied here. (C) 2013 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2013.02.025