6-N-((di-n-butylamino)-methylene)-5'-O-(4,4'-dimethoxytrityl)-L-cytidine | 271248-18-1

• 分子结构分类: 有机化合物 - 苯类化合物 - 三苯基化合物
• 英文名称: 6-N-((di-n-butylamino)-methylene)-5'-O-(4,4'-dimethoxytrityl)-L-cytidine
• 英文别名: N'-[1-[(2S,3S,4R,5S)-5-[[bis(4-methoxyphenyl)-phenylmethoxy]methyl]-3,4-dihydroxyoxolan-2-yl]-2-oxopyrimidin-4-yl]-N,N-dibutylmethanimidamide
• CAS: 271248-18-1
• 化学式: C₃₉H₄₈N₄O₇
• 分子量: 684.833
• InChiKey: DOCGEQUMBVHLKD-ZWYULGIKSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  6
• 重原子数：
  50
• 可旋转键数：
  17
• 环数：
  5.0
• sp3杂化的碳原子比例：
  0.41
• 拓扑面积：
  126
• 氢给体数：
  2
• 氢受体数：
  7

反应信息

• 作为反应物：
  描述：

  6-N-((di-n-butylamino)-methylene)-5'-O-(4,4'-dimethoxytrityl)-L-cytidine 在 咪唑 、 N-甲基咪唑 、 2,4,6-三甲基吡啶 作用下， 以 四氢呋喃 、 吡啶 为溶剂， 反应 1.0h， 生成 6-N-((di-n-butylamino)-methylene)-2'-O-tert-butyldimethylsilyl-5'-O-(4,4'-dimethoxytrityl)-L-cytidine 3'-O-(2-cyanoethyl-N,N-diisopropyl)phosphoramidite
  参考文献：
  名称：

  Synthesis and Enzymatic Digestion of an RNA Nonamer in Both Enantiomeric Forms

  摘要：

  The D- and L-RNA nonamers of the sequence r(GCUUCGGC)T have been synthesised for X-ray crystallographic purposes. In vitro digestion of the unnatural optical antipode by snake venom phosphodiesterase I takes place at an approximately 1800-fold slower rate than that of the natural D-nonamer. The digestion experiments showed-to our knowledge for the first time-that L-RNA can indeed be cleaved enzymatically when phosphodiesterase I from snake venom is used-as opposed to a number of cellular ribonucleases-which sheds an interesting light on the evolution and possibly structure/function relationship of venom versus cellular degradation enzymes. The broad substrate specificity of this enzyme could be taken advantage of to study and further optimise the resistance towards biodegradation of therapeutic L-RNA aptamers. (C) 2000 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0040-4020(00)00046-6
• 作为产物：
  描述：

  L-cytidine 在 4-二甲氨基吡啶 作用下， 以 吡啶 、 甲醇 为溶剂， 生成 6-N-((di-n-butylamino)-methylene)-5'-O-(4,4'-dimethoxytrityl)-L-cytidine
  参考文献：
  名称：

  Synthesis and Enzymatic Digestion of an RNA Nonamer in Both Enantiomeric Forms

  摘要：

  The D- and L-RNA nonamers of the sequence r(GCUUCGGC)T have been synthesised for X-ray crystallographic purposes. In vitro digestion of the unnatural optical antipode by snake venom phosphodiesterase I takes place at an approximately 1800-fold slower rate than that of the natural D-nonamer. The digestion experiments showed-to our knowledge for the first time-that L-RNA can indeed be cleaved enzymatically when phosphodiesterase I from snake venom is used-as opposed to a number of cellular ribonucleases-which sheds an interesting light on the evolution and possibly structure/function relationship of venom versus cellular degradation enzymes. The broad substrate specificity of this enzyme could be taken advantage of to study and further optimise the resistance towards biodegradation of therapeutic L-RNA aptamers. (C) 2000 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0040-4020(00)00046-6

文献信息

• Synthesis and Enzymatic Digestion of an RNA Nonamer in Both Enantiomeric Forms
  作者：Elisabeth Moyroud、Ewa Biala、Peter Strazewski

  DOI：10.1016/s0040-4020(00)00046-6

  日期：2000.3

  The D- and L-RNA nonamers of the sequence r(GCUUCGGC)T have been synthesised for X-ray crystallographic purposes. In vitro digestion of the unnatural optical antipode by snake venom phosphodiesterase I takes place at an approximately 1800-fold slower rate than that of the natural D-nonamer. The digestion experiments showed-to our knowledge for the first time-that L-RNA can indeed be cleaved enzymatically when phosphodiesterase I from snake venom is used-as opposed to a number of cellular ribonucleases-which sheds an interesting light on the evolution and possibly structure/function relationship of venom versus cellular degradation enzymes. The broad substrate specificity of this enzyme could be taken advantage of to study and further optimise the resistance towards biodegradation of therapeutic L-RNA aptamers. (C) 2000 Elsevier Science Ltd. All rights reserved.