5-azidomethylbenzene-1,3-dicarboxylate di-N-hydroxysuccinimide ester | 268539-18-0

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: 5-azidomethylbenzene-1,3-dicarboxylate di-N-hydroxysuccinimide ester
• 英文别名: Bis(2,5-dioxopyrrolidin-1-yl) 5-(azidomethyl)benzene-1,3-dicarboxylate；bis(2,5-dioxopyrrolidin-1-yl) 5-(azidomethyl)benzene-1,3-dicarboxylate
• CAS: 268539-18-0
• 化学式: C₁₇H₁₃N₅O₈
• 分子量: 415.319
• InChiKey: HPOYOTVITCKGAT-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.7
• 重原子数：
  30
• 可旋转键数：
  8
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.29
• 拓扑面积：
  142
• 氢给体数：
  0
• 氢受体数：
  10

反应信息

• 作为反应物：
  描述：

  5-azidomethylbenzene-1,3-dicarboxylate di-N-hydroxysuccinimide ester 、 在 三乙胺 作用下， 以 四氢呋喃 为溶剂， 反应 168.0h， 以47%的产率得到5-azidomethyl-N,N'-bis-1-phenylmethyl-3,5-dicarboxamide>benzene-1,3-dicarboxamide
  参考文献：
  名称：

  A comparison of biological and calorimetric analyses of multivalent glycodendrimer ligands for concanavalin A

  摘要：

  The cluster glycoside effect - the observation that multivalent glycosides bind to their polyvalent protein receptors with apparent affinities greater than those that can be rationalized solely on the basis of valency is by now a well established phenomenon. As part of a continuing effort to provide a molecular basis for the cluster glycoside effect, we report here the synthesis of two series of mannosylated dendritic ligands and their performance in a range of competitive and non-competitive binding assays, including hemeagglutination inhibition (HIA), enzyme-linked lectin assays (ELLA) and isothermal titration microcalorimetry (ITC). The first series of ligands contained a semi-rigid glycylglycine spacer and showed no significant performance enhancement in any binding studies. The second series of ligands contained a flexible tetraethylene glycol spacer; these ligands showed marked enhancements at tetravalent and hexavalent levels in both HIA (IC50=3 and <0.8 mu M, respectively) and ITC (K-A=6.2x10(4) and 1.5x10(6) M-1, respectively) studies. In all cases, the thermodynamic parameters of association are consistent with non-specific aggregation rather than enhanced lectin-ligand affinity. This conclusion is reinforced by the lack of enhancements in ligand activity observed in ELLA studies. (C) 2000 Elsevier Science I;td. All rights reserved.

  DOI：

  10.1016/s0957-4166(99)00589-3
• 作为产物：
  描述：

  N-羟基丁二酰亚胺 、 5-(azidomethyl)isophthalic acid 在 N,N'-二环己基碳二亚胺 作用下， 以 四氢呋喃 为溶剂， 反应 18.0h， 以88%的产率得到5-azidomethylbenzene-1,3-dicarboxylate di-N-hydroxysuccinimide ester
  参考文献：
  名称：

  A comparison of biological and calorimetric analyses of multivalent glycodendrimer ligands for concanavalin A

  摘要：

  The cluster glycoside effect - the observation that multivalent glycosides bind to their polyvalent protein receptors with apparent affinities greater than those that can be rationalized solely on the basis of valency is by now a well established phenomenon. As part of a continuing effort to provide a molecular basis for the cluster glycoside effect, we report here the synthesis of two series of mannosylated dendritic ligands and their performance in a range of competitive and non-competitive binding assays, including hemeagglutination inhibition (HIA), enzyme-linked lectin assays (ELLA) and isothermal titration microcalorimetry (ITC). The first series of ligands contained a semi-rigid glycylglycine spacer and showed no significant performance enhancement in any binding studies. The second series of ligands contained a flexible tetraethylene glycol spacer; these ligands showed marked enhancements at tetravalent and hexavalent levels in both HIA (IC50=3 and <0.8 mu M, respectively) and ITC (K-A=6.2x10(4) and 1.5x10(6) M-1, respectively) studies. In all cases, the thermodynamic parameters of association are consistent with non-specific aggregation rather than enhanced lectin-ligand affinity. This conclusion is reinforced by the lack of enhancements in ligand activity observed in ELLA studies. (C) 2000 Elsevier Science I;td. All rights reserved.

  DOI：

  10.1016/s0957-4166(99)00589-3

文献信息

• A comparison of biological and calorimetric analyses of multivalent glycodendrimer ligands for concanavalin A
  作者：Jayme B. Corbell、Joseph J. Lundquist、Eric J. Toone

  DOI：10.1016/s0957-4166(99)00589-3

  日期：2000.1

  The cluster glycoside effect - the observation that multivalent glycosides bind to their polyvalent protein receptors with apparent affinities greater than those that can be rationalized solely on the basis of valency is by now a well established phenomenon. As part of a continuing effort to provide a molecular basis for the cluster glycoside effect, we report here the synthesis of two series of mannosylated dendritic ligands and their performance in a range of competitive and non-competitive binding assays, including hemeagglutination inhibition (HIA), enzyme-linked lectin assays (ELLA) and isothermal titration microcalorimetry (ITC). The first series of ligands contained a semi-rigid glycylglycine spacer and showed no significant performance enhancement in any binding studies. The second series of ligands contained a flexible tetraethylene glycol spacer; these ligands showed marked enhancements at tetravalent and hexavalent levels in both HIA (IC50=3 and <0.8 mu M, respectively) and ITC (K-A=6.2x10(4) and 1.5x10(6) M-1, respectively) studies. In all cases, the thermodynamic parameters of association are consistent with non-specific aggregation rather than enhanced lectin-ligand affinity. This conclusion is reinforced by the lack of enhancements in ligand activity observed in ELLA studies. (C) 2000 Elsevier Science I;td. All rights reserved.