tetra N-phenylacetyl-kanamycin A | 1352640-83-5

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: tetra N-phenylacetyl-kanamycin A
• 英文别名: N-[[(2R,3S,4S,5R,6R)-6-[(1R,2R,3S,4R,6S)-3-[(2S,3R,4S,5S,6R)-3,5-dihydroxy-6-(hydroxymethyl)-4-[(2-phenylacetyl)amino]oxan-2-yl]oxy-2-hydroxy-4,6-bis[(2-phenylacetyl)amino]cyclohexyl]oxy-3,4,5-trihydroxyoxan-2-yl]methyl]-2-phenylacetamide
• CAS: 1352640-83-5
• 化学式: C₅₀H₆₀N₄O₁₅
• 分子量: 957.044
• InChiKey: PSNQHKZLHHNFIG-SCPPYISYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.5
• 重原子数：
  69
• 可旋转键数：
  18
• 环数：
  7.0
• sp3杂化的碳原子比例：
  0.44
• 拓扑面积：
  295
• 氢给体数：
  11
• 氢受体数：
  15

反应信息

• 作为产物：
  描述：

  phenylacetic acid N-hydroxysuccinimide ester 、 卡那霉素碱 在 碳酸氢钠 作用下， 以 水 、 N,N-二甲基甲酰胺 为溶剂， 以81%的产率得到tetra N-phenylacetyl-kanamycin A
  参考文献：
  名称：

  Selective Inhibition of Bacterial and Human Topoisomerases by N-Arylacyl O-Sulfonated Aminoglycoside Derivatives

  摘要：

  Numerous therapeutic applications have been proposed for molecules that bind heparin-binding proteins. Development of such compounds has primarily focused on optimizing the degree and orientation of anionic groups on a scaffold, but utility of these polyanions has been diminished by their typically large size and nonspecific interactions with many proteins. In this study, N-arylacyl O-sulfonated aminoglycosides were synthesized and evaluated for their ability to selectively inhibit structurally similar bacterial and human topoisomerases. It is demonstrated that the structure of the aminoglycoside and of the N-arylacyl moiety imparts selective inhibition of different topoisomerases and alters the mechanism. The results here outline a strategy that will be applicable to identifying small, structurally defined oligosaccharides that bind heparin-binding proteins with a high degree of selectivity.

  DOI：

  10.1021/ml3004507

文献信息

• Selective Inhibition of Bacterial and Human Topoisomerases by <i>N</i>-Arylacyl <i>O</i>-Sulfonated Aminoglycoside Derivatives
  作者：Amanda M. Fenner、Lisa M. Oppegard、Hiroshi Hiasa、Robert J. Kerns

  DOI：10.1021/ml3004507

  日期：2013.5.9

  Numerous therapeutic applications have been proposed for molecules that bind heparin-binding proteins. Development of such compounds has primarily focused on optimizing the degree and orientation of anionic groups on a scaffold, but utility of these polyanions has been diminished by their typically large size and nonspecific interactions with many proteins. In this study, N-arylacyl O-sulfonated aminoglycosides were synthesized and evaluated for their ability to selectively inhibit structurally similar bacterial and human topoisomerases. It is demonstrated that the structure of the aminoglycoside and of the N-arylacyl moiety imparts selective inhibition of different topoisomerases and alters the mechanism. The results here outline a strategy that will be applicable to identifying small, structurally defined oligosaccharides that bind heparin-binding proteins with a high degree of selectivity.