Aplyronine C

• 分子结构分类: 有机化合物 - 苯丙烷和聚酮 - 大环内酯类和类似物
• 英文名称: Aplyronine C
• 英文别名: [(E,3R,4R,5S,6R,9S,10S,11S)-4-acetyloxy-11-[(2S,4E,6R,8R,10E,12S,15R,16R,17R,18R,20E,22E)-16,18-dihydroxy-6,12-dimethoxy-8,11,15,17-tetramethyl-24-oxo-1-oxacyclotetracosa-4,10,20,22-tetraen-2-yl]-1-[formyl(methyl)amino]-10-hydroxy-3,5,9-trimethyldodec-1-en-6-yl] 2-(dimethylamino)propanoate
• 化学式: C₅₃H₉₀N₂O₁₂
• 分子量: 947.304
• InChiKey: BBBHWFQBKKSMGH-XXLWTVECSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  8.6
• 重原子数：
  67
• 可旋转键数：
  19
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.74
• 拓扑面积：
  182
• 氢给体数：
  3
• 氢受体数：
  13

反应信息

• 作为反应物：
  描述：

  Aplyronine C 在 盐酸 作用下， 以 1,4-二氧六环 、 水 为溶剂， 反应 1.33h， 生成
  参考文献：
  名称：

  Analysis of the aplyronine A-induced protein–protein interaction between actin and tubulin by surface plasmon resonance

  摘要：

  The antitumor macrolide aplyronine A induces protein-protein interaction (PPI) between actin and tubulin to exert highly potent biological activities. The interactions and binding kinetics of these molecules were analyzed by the surface plasmon resonance with biotinylated aplyronines or tubulin as ligands. Strong binding was observed for tubulin and actin with immobilized aplyronine A. These PPIs were almost completely inhibited by one equivalent of either aplyronine A or C, or mycalolide B. In contrast, a non-competitive actin-depolymerizing agent, latrunculin A, highly accelerated their association. Significant binding was also observed for immobilized tubulin with an actin-aplyronine A complex, and the dissociation constant K-D was 1.84 mu M. Our method could be used for the quantitative analysis of the PPIs between two polymerizing proteins stabilized with small agents. (C) 2016 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2016.04.049
• 作为产物：
  描述：

  在 氢氟酸 作用下， 以 吡啶 为溶剂， 以45%的产率得到Aplyronine C
  参考文献：
  名称：

  aplyronines B和C的绝对立体化学和合成，aplyronine A的同源物，aplyronine A是一种有效的海洋来源抗肿瘤物质

  摘要：

  对映体选择性地实现了对aplyronines B和C，aplyronine A的同类物的合成，建立了它们的立体结构。

  DOI：

  10.1016/0040-4039(95)00921-x

文献信息

• Interactions of the Antitumor Macrolide Aplyronine A with Actin and Actin-Related Proteins Established by Its Versatile Photoaffinity Derivatives
  作者：Masaki Kita、Yuichiro Hirayama、Kota Yamagishi、Kozo Yoneda、Ryosuke Fujisawa、Hideo Kigoshi

  DOI：10.1021/ja310495p

  日期：2012.12.19

  The antitumor and apoptogenic macrolide aplyronine A (ApA) is a potent actin-depolymerizing agent. We developed an ApA acetylene analog that bears the aryldiazirine group at the C34 terminus, which formed a covalent bond with actin. With the use of the photoaffinity biotin derivatives of aplyronines A and C, Arp2 and Arp3 (actin-related proteins) were specifically purified as binding proteins along

  抗肿瘤和凋亡大环内酯 aplyronine A (ApA) 是一种有效的肌动蛋白解聚剂。我们开发了一种在 C34 末端带有芳基二氮丙啶基团的 ApA 乙炔类似物，它与肌动蛋白形成共价键。使用 aplyronines A 和 C 的光亲和生物素衍生物，Arp2 和 Arp3（肌动蛋白相关蛋白）与来自肿瘤细胞裂解物的肌动蛋白一起被特异性纯化为结合蛋白。然而，Arp2 和 Arp3 不与 aplyronine 光亲和衍生物共价结合。因此，肌动蛋白相关蛋白可能作为肌动蛋白/ApA 复合物的三元加合物或通过寡聚肌动蛋白间接结合到 ApA。
• Absolute stereochemistry and synthesis of aplyronines B and C, the congeners of aplyronine A, a potent antitumor substance of marine origin
  作者：Kiyotake Suenaga、Takeshi Ishigaki、Akira Sakakura、Hideo Kigoshi、Kiyoyuki Yamada

  DOI：10.1016/0040-4039(95)00921-x

  日期：1995.7

  Synthesis of aplyronines B and C, the congeners of aplyronine A, was achieved enantioselectively, which established their stereostructures.

  对映体选择性地实现了对aplyronines B和C，aplyronine A的同类物的合成，建立了它们的立体结构。
• Analysis of the aplyronine A-induced protein–protein interaction between actin and tubulin by surface plasmon resonance
  作者：Yuichiro Hirayama、Kota Yamagishi、Tomohiro Suzuki、Hirokazu Kawagishi、Masaki Kita、Hideo Kigoshi

  DOI：10.1016/j.bmc.2016.04.049

  日期：2016.6

  The antitumor macrolide aplyronine A induces protein-protein interaction (PPI) between actin and tubulin to exert highly potent biological activities. The interactions and binding kinetics of these molecules were analyzed by the surface plasmon resonance with biotinylated aplyronines or tubulin as ligands. Strong binding was observed for tubulin and actin with immobilized aplyronine A. These PPIs were almost completely inhibited by one equivalent of either aplyronine A or C, or mycalolide B. In contrast, a non-competitive actin-depolymerizing agent, latrunculin A, highly accelerated their association. Significant binding was also observed for immobilized tubulin with an actin-aplyronine A complex, and the dissociation constant K-D was 1.84 mu M. Our method could be used for the quantitative analysis of the PPIs between two polymerizing proteins stabilized with small agents. (C) 2016 Elsevier Ltd. All rights reserved.