O-(3,4,6-tri-O-acetyl-2-azido-2-deoxy-α-D-galactopyranosyl)-N-[(9H-fluoren-9-yl)-methoxycarbonyl]-trans-L-hydroxyproline tert-butyl ester | 1415099-15-8

• 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: O-(3,4,6-tri-O-acetyl-2-azido-2-deoxy-α-D-galactopyranosyl)-N-[(9H-fluoren-9-yl)-methoxycarbonyl]-trans-L-hydroxyproline tert-butyl ester
• 英文别名: O-(3,4,6-tri-O-acetyl-2-azido-2-deoxy-D-galactopyranosyl)-N-[(9H-fluoren-9-yl)-methoxycarbonyl]-(4R)-L-hydroxyproline tert-butyl ester
• CAS: 1415099-15-8
• 化学式: C₃₆H₄₂N₄O₁₂
• 分子量: 722.749
• InChiKey: UIIMKNVVBIRSIU-KVGGOZCISA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.57
• 重原子数：
  52.0
• 可旋转键数：
  10.0
• 环数：
  5.0
• sp3杂化的碳原子比例：
  0.53
• 拓扑面积：
  201.96
• 氢给体数：
  0.0
• 氢受体数：
  13.0

反应信息

• 作为产物：
  描述：

  3,4,6-tri-O-acetyl-2-azido-2-deoxy-α-D-galactopyranosyl chloride 、 Fmoc-Hyp-OtBu 在 silver carbonate 、 silver perchlorate 作用下， 以 二氯甲烷 、 甲苯 为溶剂， 反应 41.0h， 以81.818%的产率得到
  参考文献：
  名称：

  AFGP合成物中类似物的序列修饰和碳水化合物变化对构象和抗冻活性的影响

  摘要：

  某些北极和南极等温物种已经制定了在低温条件下生存的策略，其中包括抗冻糖肽（AFGP）。AFGP形成一类生物防冻剂，具有在体外和体内抑制冰生长的能力，因此能够在低于冰点的温度下维持生命。AFGP通常由不同数量的（Ala-Ala-Thr）n单位（n = 4-55）组成，其中二糖β- D-半乳糖基-（1→3）-α- N-乙酰基-D-半乳糖胺糖基连接至每个苏氨酸侧链羟基。已经证明AFGP采用聚脯氨酸II螺旋构象。尽管这种模式在不同物种之间是高度保守的，但通常会发生与氨基酸组成有关的微异质性。例如，在较小的AFGP中，丙氨酸偶尔会被脯氨酸取代。通过脯氨酸取代丙氨酸和糖基化羟脯氨酸糖基化苏氨酸来研究次要和主要序列突变对AFGP类似物构象和抗冻活性的影响。通过使用微波增强固相肽合成制备目标化合物。此外，通过铜催化的叠氮化物-炔烃环加成反应（CuAAC）获得了人工类似物：n个单位（ n = 2-4）包含4

  DOI：

  10.1002/chem.201202119

文献信息

• Synthesis of peptides and glycopeptides with polyproline II helical topology as potential antifreeze molecules
  作者：Leo Corcilius、Gajan Santhakumar、Robin S. Stone、Chantelle J. Capicciotti、Soumya Joseph、Jacqueline M. Matthews、Robert N. Ben、Richard J. Payne

  DOI：10.1016/j.bmc.2013.02.025

  日期：2013.6

  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.