N⁴,N^5'-bis(3-((3s,5s,7s)-adamantan-1-ylamino)-3-oxopropyl)-[2,3'-bipyridine]-4,5'-dicarboxamide | 1330577-33-7

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 吡啶及其衍生物
• 英文名称: N⁴,N^5'-bis(3-((3s,5s,7s)-adamantan-1-ylamino)-3-oxopropyl)-[2,3'-bipyridine]-4,5'-dicarboxamide
• 英文别名: N-[3-(1-adamantylamino)-3-oxopropyl]-2-[4-[[3-(1-adamantylamino)-3-oxopropyl]carbamoyl]pyridin-2-yl]pyridine-4-carboxamide
• CAS: 1330577-33-7
• 化学式: C₃₈H₄₈N₆O₄
• 分子量: 652.837
• InChiKey: IXEJAMIXFRYAMV-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.9
• 重原子数：
  48
• 可旋转键数：
  11
• 环数：
  10.0
• sp3杂化的碳原子比例：
  0.63
• 拓扑面积：
  142
• 氢给体数：
  4
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  顺-双(2,2'-二吡啶基)二氯化钌(II)二水合物 、 N⁴,N^5'-bis(3-((3s,5s,7s)-adamantan-1-ylamino)-3-oxopropyl)-[2,3'-bipyridine]-4,5'-dicarboxamide 以 乙醇 为溶剂， 以20%的产率得到[Ru(bipy)2((C5H3NCONHC2H4CONHC10H15)2)](2+)
  参考文献：
  名称：

  Hexameric Supramolecular Scaffold Orients Carbohydrates To Sense Bacteria

  摘要：

  Carbohydrates are integral to biological signaling networks and cell-cell interactions, yet the detection of discrete carbohydrate-lectin interactions remains difficult since binding is generally weak. A strategy to overcome this problem is to create multivalent sensors, where the avidity rather than the affinity of the interaction is important. Here we describe the development of a series of multivalent sensors that self-assemble via hydrophobic supramolecular interactions. The multivalent sensors are comprised of a fluorescent ruthenium(II) core surrounded by a heptarnannosylated beta-cyclodextrin scaffold. Two additional series of complexes were synthesized as proof-of-principle for supramolecular self-assembly, the fluorescent core alone and the core plus beta-cydodextrin. Spectroscopic analyses confirmed that the three mannosylated sensors displayed 14, 28, and 42 sugar units, respectively. Each complex adopted original and unique spatial arrangements. The sensors were used to investigate the influence of carbohydrate spatial arrangement and clustering on the mechanistic and qualitative properties of lectin binding. Simple visualization of binding between a fluorescent, multivalent mannose complex and the Escherichia coli strain ORN178 that possesses mannose-specific receptor sites illustrates the potential for these complexes as biosensors.

  DOI：

  10.1021/ja2036767
• 作为产物：
  描述：

  2,2'-联吡啶-4,4'-二甲酸 在 氯化亚砜 、 三乙胺 作用下， 以 二氯甲烷 为溶剂， 反应 72.08h， 生成 N⁴,N^5'-bis(3-((3s,5s,7s)-adamantan-1-ylamino)-3-oxopropyl)-[2,3'-bipyridine]-4,5'-dicarboxamide
  参考文献：
  名称：

  Hexameric Supramolecular Scaffold Orients Carbohydrates To Sense Bacteria

  摘要：

  Carbohydrates are integral to biological signaling networks and cell-cell interactions, yet the detection of discrete carbohydrate-lectin interactions remains difficult since binding is generally weak. A strategy to overcome this problem is to create multivalent sensors, where the avidity rather than the affinity of the interaction is important. Here we describe the development of a series of multivalent sensors that self-assemble via hydrophobic supramolecular interactions. The multivalent sensors are comprised of a fluorescent ruthenium(II) core surrounded by a heptarnannosylated beta-cyclodextrin scaffold. Two additional series of complexes were synthesized as proof-of-principle for supramolecular self-assembly, the fluorescent core alone and the core plus beta-cydodextrin. Spectroscopic analyses confirmed that the three mannosylated sensors displayed 14, 28, and 42 sugar units, respectively. Each complex adopted original and unique spatial arrangements. The sensors were used to investigate the influence of carbohydrate spatial arrangement and clustering on the mechanistic and qualitative properties of lectin binding. Simple visualization of binding between a fluorescent, multivalent mannose complex and the Escherichia coli strain ORN178 that possesses mannose-specific receptor sites illustrates the potential for these complexes as biosensors.

  DOI：

  10.1021/ja2036767

文献信息

• Supramolecular metalloglycodendrimers selectively modulate lectin binding and delivery of Ru(<scp>ii</scp>) complexes into mammalian cells
  作者：Harikrishna Bavireddi、Raghavendra Vasudeva Murthy、Madhuri Gade、Sivakoti Sangabathuni、Raghavendra Kikkeri

  DOI：10.1039/c6ob01546h

  日期：——

  Host–guest interactions was used for controlled delivery of the Ru(ii)-glycodendrimers into cancer cells to induce cytotoxicity by reacting with the endoplasmic reticulum.

  宿主-客体相互作用被用于将Ru(ii)-glycodendrimers控制释放到癌细胞中，通过与内质网反应诱导细胞毒性。
• Hexameric Supramolecular Scaffold Orients Carbohydrates To Sense Bacteria
  作者：Dan Grünstein、Maha Maglinao、Raghavendra Kikkeri、Mayeul Collot、Konstantin Barylyuk、Bernd Lepenies、Faustin Kamena、Renato Zenobi、Peter H. Seeberger

  DOI：10.1021/ja2036767

  日期：2011.9.7

  Carbohydrates are integral to biological signaling networks and cell-cell interactions, yet the detection of discrete carbohydrate-lectin interactions remains difficult since binding is generally weak. A strategy to overcome this problem is to create multivalent sensors, where the avidity rather than the affinity of the interaction is important. Here we describe the development of a series of multivalent sensors that self-assemble via hydrophobic supramolecular interactions. The multivalent sensors are comprised of a fluorescent ruthenium(II) core surrounded by a heptarnannosylated beta-cyclodextrin scaffold. Two additional series of complexes were synthesized as proof-of-principle for supramolecular self-assembly, the fluorescent core alone and the core plus beta-cydodextrin. Spectroscopic analyses confirmed that the three mannosylated sensors displayed 14, 28, and 42 sugar units, respectively. Each complex adopted original and unique spatial arrangements. The sensors were used to investigate the influence of carbohydrate spatial arrangement and clustering on the mechanistic and qualitative properties of lectin binding. Simple visualization of binding between a fluorescent, multivalent mannose complex and the Escherichia coli strain ORN178 that possesses mannose-specific receptor sites illustrates the potential for these complexes as biosensors.