O-(2-acetamido-2-deoxy-β-D-glucopyranosyl)hydroxylamine | 195970-62-8

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: O-(2-acetamido-2-deoxy-β-D-glucopyranosyl)hydroxylamine
• 英文别名: N-[(2S,3R,4R,5S,6R)-2-aminooxy-4,5-dihydroxy-6-(hydroxymethyl)oxan-3-yl]acetamide
• CAS: 195970-62-8
• 化学式: C₈H₁₆N₂O₆
• 分子量: 236.225
• InChiKey: XRZLVHCKXHEMGA-PVFLNQBWSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -2.2
• 重原子数：
  16
• 可旋转键数：
  3
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.88
• 拓扑面积：
  134
• 氢给体数：
  5
• 氢受体数：
  7

反应信息

• 作为反应物：
  描述：

  O-(2-acetamido-2-deoxy-β-D-glucopyranosyl)hydroxylamine 在 β-1,4-galactosyltransferase 、 α-2,3-sialyltransferase 、 manganese(ll) chloride 、 alkaline phosphatase 作用下， 反应 96.0h， 生成 NeuAc(a2-3)Gal(b1-4)GlcNAc(b)-O-NH2
  参考文献：
  名称：

  A Method for the Generation of Glycoprotein Mimetics

  摘要：

  A general method for preparing glycoprotein mimetics with defined glycan structure using the Z domain protein as an example is reported. An unnatural amino acid containing the keto group was site-specifically incorporated into a target protein, Z domain, in response to the amber nonsense codon with high translational fidelity and efficiency. An aminooxy saccharide derivative was then selectively coupled to this genetically encoded keto group. The resulting saccharide core was elaborated to a glycan complex with glycosyltransferases. Alternatively, aminooxy analogues of more complicated glycans were prepared and directly attached to the keto group. Homogeneous glycoprotein mimetics thus prepared should prove useful for the study of carbohydrate effects on glycoprotein structure and function. This method may also lead to the production of glycoprotein therapeutics from Escherichia coli.

  DOI：

  10.1021/ja029433n
• 作为产物：
  描述：

  O-(2-acetamido-3,4,6-tri-O-acetyl-2-deoxy-β-D-glucopyranosyl)-N-hydroxysuccinimide 在 一水合肼 、 aminopropyl silica gel 作用下， 生成 O-(2-acetamido-2-deoxy-β-D-glucopyranosyl)hydroxylamine
  参考文献：
  名称：

  Aminooxy-, Hydrazide-, and Thiosemicarbazide-Functionalized Saccharides:  Versatile Reagents for Glycoconjugate Synthesis

  摘要：

  DOI：

  10.1021/jo981351n

文献信息

• Tetravalent glycocyclopeptide with nanomolar affinity to wheat germ agglutinin
  作者：Michele Fiore、Nathalie Berthet、Alberto Marra、Emilie Gillon、Pascal Dumy、Alessandro Dondoni、Anne Imberty、Olivier Renaudet

  DOI：10.1039/c3ob41203b

  日期：——

  functionalized with GlcNAc was synthesized using copper(I)-catalysed alkyne–azide cycloaddition, oxime ligation and thiol–ene coupling. The binding ability of these compounds towards wheat germ agglutinin was studied by a competitive ELLA test and ITC experiments. While all compounds were able to inhibit WGA binding to GlcNAc-polymer coated surfaces at low concentrations, derivative 17 having an aliphatic spacer

  使用铜（I）催化的炔-叠氮化物环加成，肟连接和硫醇-烯偶联合成了一系列用GlcNAc功能化的四价糖环肽。通过竞争性ELLA试验和ITC实验研究了这些化合物对小麦胚芽凝集素的结合能力。尽管所有化合物都能在低浓度下抑制WGA结合到GlcNAc聚合物涂层的表面，但具有脂肪族间隔基和硫醚键的衍生物17的单糖效力比GlcNAc高4.9×10 6倍。ITC实验证实了这一非常强的效果，因为这些实验表明该化合物的缔合常数为9 nM，因此比GlcNAc的合成增益高20万倍。这些结果对于化合物图17代表报道的WGA的最高结合性质。
• Aminooxy-, Hydrazide-, and Thiosemicarbazide-Functionalized Saccharides:  Versatile Reagents for Glycoconjugate Synthesis
  作者：Elena C. Rodriguez、Lisa A. Marcaurelle、Carolyn R. Bertozzi

  DOI：10.1021/jo981351n

  日期：1998.10.1
• A Method for the Generation of Glycoprotein Mimetics
  作者：Haitian Liu、Lei Wang、Ansgar Brock、Chi-Huey Wong、Peter G. Schultz

  DOI：10.1021/ja029433n

  日期：2003.2.19

  A general method for preparing glycoprotein mimetics with defined glycan structure using the Z domain protein as an example is reported. An unnatural amino acid containing the keto group was site-specifically incorporated into a target protein, Z domain, in response to the amber nonsense codon with high translational fidelity and efficiency. An aminooxy saccharide derivative was then selectively coupled to this genetically encoded keto group. The resulting saccharide core was elaborated to a glycan complex with glycosyltransferases. Alternatively, aminooxy analogues of more complicated glycans were prepared and directly attached to the keto group. Homogeneous glycoprotein mimetics thus prepared should prove useful for the study of carbohydrate effects on glycoprotein structure and function. This method may also lead to the production of glycoprotein therapeutics from Escherichia coli.