N,N'-bis-(4-(2-acetamido-2-deoxy-β-D-glucopyranosyloxy)-(Z)-but-2-enyloxycarbonyl)-p-xylylenediamine | 959924-04-0

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: N,N'-bis-(4-(2-acetamido-2-deoxy-β-D-glucopyranosyloxy)-(Z)-but-2-enyloxycarbonyl)-p-xylylenediamine
• 英文别名: [(Z)-4-[(2R,3R,4R,5S,6R)-3-acetamido-4,5-dihydroxy-6-(hydroxymethyl)oxan-2-yl]oxybut-2-enyl] N-[[4-[[[(Z)-4-[(2R,3R,4R,5S,6R)-3-acetamido-4,5-dihydroxy-6-(hydroxymethyl)oxan-2-yl]oxybut-2-enoxy]carbonylamino]methyl]phenyl]methyl]carbamate
• CAS: 959924-04-0
• 化学式: C₃₄H₅₀N₄O₁₆
• 分子量: 770.788
• InChiKey: DDYLZYWCXSPXRF-HQBIZHESSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -3
• 重原子数：
  54
• 可旋转键数：
  20
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.59
• 拓扑面积：
  293
• 氢给体数：
  10
• 氢受体数：
  16

反应信息

• 作为产物：
  描述：

  N,N'-bis-(4-(2-acetamido-3,4,6-tri-O-acetyl-2-deoxy-β-D-glucopyranosyloxy)-(Z)-but-2-enyloxycarbonyl)-p-xylylenediamine 在 sodium methylate 作用下， 以 甲醇 为溶剂， 反应 2.5h， 以99%的产率得到N,N'-bis-(4-(2-acetamido-2-deoxy-β-D-glucopyranosyloxy)-(Z)-but-2-enyloxycarbonyl)-p-xylylenediamine
  参考文献：
  名称：

  Probing multivalent carbohydrate–lectin interactions by an enzyme-linked lectin assay employing covalently immobilized carbohydrates

  摘要：

  We report here the synthesis of a series of mono-to trivalent N-acetylglucosamine (GlcNAc) derivatives as ligands for the plant lectin wheat germ agglutinin (WGA). Their WGA binding potencies were determined by an established enzyme-linked lectin assay (ELLA) employing microtiter plates with non-covalently immobilized porcine stomach mucin (PSM) as reference ligand and an ELLA with a new GlcNAc derivative covalently immobilized via a thiourea linkage. Comparison of both assays revealed that the type of presentation of GlcNAc residues on the microtiter plates either as part of a glycoprotein or as a covalently immobilized monosaccharide derivative strongly influences the outcome of the assay. Although the apparent dissociation constants K-D(ELLA) D for the interaction of peroxidase-labeled WGA with the microtiter plates are comparable for both surfaces, IC50 values obtained with the PSM-free ELLA were substantially lower. Even more strikingly, this ELLA displayed a better differentiation between ligands of different valency leading to significantly higher relative inhibitory potencies of multivalent ligands compared to monovalent. Additionally, problems associated with the use of PSM, such as maximum inhibition at considerably less than 100% and poor reproducibility of IC50 values could be overcome with this type of ELLA. (c) 2007 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2007.08.063

文献信息

• Probing multivalent carbohydrate–lectin interactions by an enzyme-linked lectin assay employing covalently immobilized carbohydrates
  作者：Caroline Maierhofer、Katja Rohmer、Valentin Wittmann

  DOI：10.1016/j.bmc.2007.08.063

  日期：2007.12

  We report here the synthesis of a series of mono-to trivalent N-acetylglucosamine (GlcNAc) derivatives as ligands for the plant lectin wheat germ agglutinin (WGA). Their WGA binding potencies were determined by an established enzyme-linked lectin assay (ELLA) employing microtiter plates with non-covalently immobilized porcine stomach mucin (PSM) as reference ligand and an ELLA with a new GlcNAc derivative covalently immobilized via a thiourea linkage. Comparison of both assays revealed that the type of presentation of GlcNAc residues on the microtiter plates either as part of a glycoprotein or as a covalently immobilized monosaccharide derivative strongly influences the outcome of the assay. Although the apparent dissociation constants K-D(ELLA) D for the interaction of peroxidase-labeled WGA with the microtiter plates are comparable for both surfaces, IC50 values obtained with the PSM-free ELLA were substantially lower. Even more strikingly, this ELLA displayed a better differentiation between ligands of different valency leading to significantly higher relative inhibitory potencies of multivalent ligands compared to monovalent. Additionally, problems associated with the use of PSM, such as maximum inhibition at considerably less than 100% and poor reproducibility of IC50 values could be overcome with this type of ELLA. (c) 2007 Elsevier Ltd. All rights reserved.