O-(2,4,6-tri-O-acetyl-β-D-galactopyranosyl)-(1->4)-2,3,6-tri-O-acetyl-1-β-D-glucopyranosyl azide | 226707-92-2

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: O-(2,4,6-tri-O-acetyl-β-D-galactopyranosyl)-(1->4)-2,3,6-tri-O-acetyl-1-β-D-glucopyranosyl azide
• 英文别名: O-(2,4,6-tri-O-acetyl-β-D-galactopyranosyl)-(1->4)-2,3,4-tri-O-acetyl-β-D-glucopyranosyl azide；(2,4,6-tri-O-acetyl-β-D-galactopyranosyl)-(1->4)-2,3,6-tri-O-acetyl-β-D-glucopyranosyl azide
• CAS: 226707-92-2
• 化学式: C₂₄H₃₃N₃O₁₆
• 分子量: 619.537
• InChiKey: YSSTXGCYYQQZIQ-RBTXJNGRSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.65
• 重原子数：
  43.0
• 可旋转键数：
  11.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.75
• 拓扑面积：
  254.48
• 氢给体数：
  1.0
• 氢受体数：
  17.0

反应信息

• 作为反应物：
  描述：

  O-(2,4,6-tri-O-acetyl-β-D-galactopyranosyl)-(1->4)-2,3,6-tri-O-acetyl-1-β-D-glucopyranosyl azide 在 platinum(IV) oxide 、 palladium on activated charcoal 吡啶 、 4-二甲氨基吡啶 、 sodium azide 、 4 A molecular sieve 、 氢气 、 sodium methylate 、 三乙胺 作用下， 以 甲醇 、 二氯甲烷 、 N,N-二甲基甲酰胺 为溶剂， -30.0~70.0 ℃ 、405.3 kPa 条件下， 反应 27.0h， 生成 N-[O-(β-D-galactopyranosyl)-(1->4)-1-β-D-glucopyranosyl]-5-aminopentamide
  参考文献：
  名称：

  Enhanced Inhibition of Human Anti-Gal Antibody Binding to Mammalian Cells by Synthetic α-Gal Epitope Polymers

  摘要：

  Neoglycopolymers of polyacrylamide backbone conjugated with varying densities of Gal alpha 1-3Gal beta 1-4Glc beta trisaccharide epitopes (alpha-Gal epitopes) were designed and synthesized to study the inhibition of the binding of human natural anti-Gal antibodies to either alpha-Gal-containing glycoproteins or alpha-Gal antigens on the surface of mammalian cells. An inhibition ELISA using mouse laminin and a flow cytometry assay using pig kidney cells (PK15) were established to determine the binding affinity of the synthesized polymers. In comparison to the alpha-Gal monomer (Gal alpha 1-3Gal beta 1-4GlcNHAc beta), the alpha-Gal polymers dramatically enhanced the inhibition of human anti-Gal antibodies (IgG, IgM, and IgA) binding to mouse laminin or mammalian cells. Increases of 7.8 x 10(3)- and 5.0 x 10(4) -fold in inhibitory potential of polymer 7C to IgA and IgM (with IC(50)s of 7.0 and 5.6 nM respectively) were observed over the monomer in inhibition ELISA. The results also indicated that binding enhancement of alpha-Gal polymers is greater for anti-Gal IgA and IgM than for IgG. Such amplified binding differences among the three anti-Gal isotypes can be utilized to selectively inhibit or remove a particular isotype of anti-Gal antibodies. Moreover, it was demonstrated through the flow cytometry assay that certain alpha-Gal polymers are effective in inhibition of anti-Gal antibody (in human serum) binding to pig kidney (PK15) cells. Thus, such synthetic carbohydrate polymers may find practical applications in cell xenotransplantations.

  DOI：

  10.1021/ja990219h
• 作为产物：
  描述：

  [3-O-(4-methoxybenzyl) 2,4,6-tri-O-acetyl-β-D-galactopyranosyl]-(1->4)-2,3,6-tri-O-acetyl-β-D-glucopyranosyl azide 在 ammonium cerium(IV) nitrate 作用下， 以 水 、 乙腈 为溶剂， 以90%的产率得到O-(2,4,6-tri-O-acetyl-β-D-galactopyranosyl)-(1->4)-2,3,6-tri-O-acetyl-1-β-D-glucopyranosyl azide
  参考文献：
  名称：

  Large Scale Synthesis of A Derivative of An α-Galactosyl Trisaccharide Epitope Involved in the Hyperacute Rejection of Xenotransplantation

  摘要：

  A derivative of an alpha-galactosyl trisaccharide xenoactive antigen, (2,3,4,6-tetra-O-benzyl-alpha-D-galactopyranosyl)-(1-->3)-(2,4,6-tri-O-acetyl-beta-D-galactopyranosyl)-(1-->4)-2,3,6-tri-O-acetyl-beta-D-glucopyranosyl azide (5), was synthesized on a large scale (50 gram). The synthesis involved a high yielding and highly stereoselective (alpha \beta>20:1) glycosylation reaction utilizing a thiogalactoside as the donor and a selectively protected lactose azide as the acceptor. This derivative serves as a versatile intermediate that can be transformed into a variety of alpha-Gal containing glycoconjugates highly desired in xenotransplantation research and pharmaceutical development.

  DOI：

  10.1080/07328309908544050

文献信息

• The synthesis of deoxy-α-Gal epitope derivatives for the evaluation of an anti-α-Gal antibody binding
  作者：Adam J. Janczuk、Wei Zhang、Peter R. Andreana、Joshua Warrick、Peng G. Wang

  DOI：10.1016/s0008-6215(02)00159-3

  日期：2002.8

  alpha-Gal epitopes (also termed as alpha-Gal) are carbohydrate structures bearing the alpha-D-Gal-(1 --> 3)-beta-D-Gal terminus 1 and are known to be the antigen responsible for antibody-mediated hyperacute rejection in xenotransplantation. Terminal 2-, 3-, 4-, and 6-deoxy-Gal derivatives of alpha-Gal were synthesized. Inhibition ELISA using mouse laminin was established to determine the binding affinity of the synthesized alpha-Gal derivatives. 4-Deoxy-alpha-Gal derivative 7 showed a significant reduction in antibody recognition. The IC50 value was 15-fold poorer than the standard alpha-Gal epitopes alpha-D-Gal-(1 --> 3)-beta-D-Gal-(1 --> 4)-beta-D-Glc-NHAc (39) and alpha-D-Gal-(1 --> 3)-beta-D-Gal-(1 -- 4)-beta-D-Glc-OBn (40). A similar observation was seen with 2-deoxy-alpha-Gal derivative 5, whose IC50 value was nearly tenfold higher than the standards. Interestingly, substitution at the terminal 3-position resulted in only a fourfold decrease in antibody recognition, suggesting a possible point of future derivation. Finally, 6-deoxy-alpha-Gal derivative 8 exhibited similar antibody recognition to both alpha-Gal epitope 39 and alpha-Gal epitope 40. This strongly suggests that derivatization at the 6-position can be accomplished without loss of antibody recognition. These findings can be utilized for the future design of other alpha-Gal derivatives. (C) 2002 Elsevier Science Ltd. All rights reserved.
• A Unique Chemoenzymatic Synthesis of α-Galactosyl Epitope Derivatives Containing Free Amino Groups:  Efficient Separation and Further Manipulation
  作者：Jianwen Fang、Xi Chen、Wei Zhang、Jianqiang Wang、Peter R. Andreana、Peng George Wang

  DOI：10.1021/jo990159y

  日期：1999.5.1

  A novel. chemoenzymatic approach for the synthesis of oligosacchrides containing free amino groups has been developed in which thermophilic glycosidases and a fusion enzyme containing catalytic domains of uridine-5'-diphospho-galactose 4-epimerase and alpha(1-->3) galactosyltransferase were used. This methodology, in conjunction with a convenient purification procedure employing ion exchange chromatography, facilitates the lengthy and high-cost process of carbohydrate synthesis. The prepared oligosaccharides range from disaccharide lactosamine (1a), trisaccharide alpha-Gal-(1-->3)-beta-Gal-(1-->4)-GlcNH(2) (2), tetrasaccharide beta-Gal-(1-->4)-beta-GlcNH(2)-(1-->3)-beta-Gal-(1-->4)-beta-Glc-N-3 (7), to pentasaccharide alpha-Gal-(1-->3)-beta-Gal-(1-->4)-beta-GlcNH(2)-(1-->3)-beta-Gal-(1-->4)-beta-Glc-N-3 (15). Compounds 2 and 15 are derivatives of natural alpha-Gal epitopes. Both of them have shown comparable activities with their natural parent compounds toward human anti-Gal IgG. This method provides a practical approach for the preparation and purification of oligosaccharides containing free amino groups, which can be further derivatized for the enhancement of biological activities.