| 176747-10-7

• 分子结构分类: 有机化合物 - 核苷、核苷酸和类似物 - 嘌呤核苷酸
• CAS: 176747-10-7
• 化学式: C₅₆H₁₀₅N₈O₉P
• 分子量: 1065.47
• InChiKey: LGFUFVAPZLGXSW-HAYBSPKOSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  12.36
• 重原子数：
  74.0
• 可旋转键数：
  49.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.88
• 拓扑面积：
  247.51
• 氢给体数：
  7.0
• 氢受体数：
  13.0

反应信息

• 作为反应物：
  描述：

  在 六甲基磷酰三胺 、 三辛胺 、 氯磷酸二苯酯 、 tri-n-butylamine pyrophosphate 作用下， 生成 [[(2R,3S,4R,5R)-5-[6-amino-8-[6-[[4-(dioctadecylamino)-4-oxobutanoyl]amino]hexylamino]purin-9-yl]-3,4-dihydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl] phosphono hydrogen phosphate
  参考文献：
  名称：

  ATP-LipidsProtein Anchor and Energy Source in Two Dimensions

  摘要：

  The ubiquitous function of ATP as energy equivalent in nature has resulted in a common folding pattern of ATP-binding proteins. Their binding pocket tolerates modifications of the adenine ring to some extend, whereas those of the triphosphate group strongly affect the binding affinity. In consequence, immobilized C8- and N-6- modified ATP analogues are frequently used for affinity purification of ATPases or kinases. To combine this unique recognition principle with the fascinating properties of self-assembly, we have synthesized a novel class of hydrolyzable and nonhydrolyzable ATP-lipids where the nucleotides are covalently attached via C8- or N-6-position of the adenine ring to a synthetic lipid. These ATP-lipids were characterized by various enzyme assays in micellar solution, resulting in ATPase and competition activities that are comparable to their free counterparts. The specific docking of actin as a model of an ATP-binding protein to ATP-lipid monolayers was followed by film balance technique and epifluorescence microscopy. Based on this specific interaction, actin-supported membranes were generated to study shape transitions of vesicular systems. Due to the coupling of actin to ATP-lipid bilayers drastic changes in the viscoelastic properties and shape transitions were observed by phase contrast microscopy. These results underline the properties of these novel ATP-lipids as protein anchor or energy source in two dimensions. They can be applied either to form phantom cells, actin-supported membranes or to orient and crystallize ATP-binding proteins at lipid interfaces.

  DOI：

  10.1021/ja953937m
• 作为产物：
  描述：

  8-bromo-2',3'-O-isopropylene adenosine 在 2,6-二甲基吡啶 、 lead(IV) acetate 、 硫酸 、 三乙胺 作用下， 以 1,4-二氧六环 、 甲醇 、 氯仿 、 水 为溶剂， 反应 6.0h， 生成
  参考文献：
  名称：

  ATP-LipidsProtein Anchor and Energy Source in Two Dimensions

  摘要：

  The ubiquitous function of ATP as energy equivalent in nature has resulted in a common folding pattern of ATP-binding proteins. Their binding pocket tolerates modifications of the adenine ring to some extend, whereas those of the triphosphate group strongly affect the binding affinity. In consequence, immobilized C8- and N-6- modified ATP analogues are frequently used for affinity purification of ATPases or kinases. To combine this unique recognition principle with the fascinating properties of self-assembly, we have synthesized a novel class of hydrolyzable and nonhydrolyzable ATP-lipids where the nucleotides are covalently attached via C8- or N-6-position of the adenine ring to a synthetic lipid. These ATP-lipids were characterized by various enzyme assays in micellar solution, resulting in ATPase and competition activities that are comparable to their free counterparts. The specific docking of actin as a model of an ATP-binding protein to ATP-lipid monolayers was followed by film balance technique and epifluorescence microscopy. Based on this specific interaction, actin-supported membranes were generated to study shape transitions of vesicular systems. Due to the coupling of actin to ATP-lipid bilayers drastic changes in the viscoelastic properties and shape transitions were observed by phase contrast microscopy. These results underline the properties of these novel ATP-lipids as protein anchor or energy source in two dimensions. They can be applied either to form phantom cells, actin-supported membranes or to orient and crystallize ATP-binding proteins at lipid interfaces.

  DOI：

  10.1021/ja953937m