N⁶-benzoylnoraristeromycin | 150018-18-1

• 分子结构分类: 有机化合物 - 核苷、核苷酸和类似物 - 核苷和核苷酸类似物
• 英文名称: N⁶-benzoylnoraristeromycin
• 英文别名: 9-[(1'R,2'S,3'R,4'S)-2',3',4'-trihydroxycyclopentan-1'-yl]-9-H-N⁶-benzoyladenine；N-[9-[(1R,2S,3R,4S)-2,3,4-trihydroxycyclopentyl]purin-6-yl]benzamide
• CAS: 150018-18-1
• 化学式: C₁₇H₁₇N₅O₄
• 分子量: 355.353
• InChiKey: BFHIVQDVFRGSRZ-UVLXDEKHSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.2
• 重原子数：
  26
• 可旋转键数：
  3
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.29
• 拓扑面积：
  133
• 氢给体数：
  4
• 氢受体数：
  7

反应信息

• 作为反应物：
  描述：

  N⁶-benzoylnoraristeromycin 在 甲醇 、 4-二甲氨基吡啶 、 叠氮化锂 、 氨 、 三乙胺 、 原甲酸三乙酯 、 三氟乙酸 作用下， 以 二氯甲烷 、 N,N-二甲基甲酰胺 为溶剂， 反应 3.25h， 生成 (-)-9β-(2'α,3'α-dihydroxypent-4'-enyl)adenine
  参考文献：
  名称：

  Facile synthesis of 9-[(1′R,2′S)-2′-hydroxy-3′-oxocyclopentan-1′-yl]-9-H-adenine possessing inhibitory activity against human recombinant S-adenosyl-l-homocysteine hydrolase

  摘要：

  Treatment of 4'-O-methanesulfonyl-2',3'-O-isopropylideneoraisteromycin with KOBut gave the corresponding 3',4'-dehydro derivative, and subsequent deprotection resulted in the formation of 9-[(1'R,2'S)-2'-hydroxy-3'-oxocyclopentan-1'-yl]-9-H-adenine possessing inhibitory activity against human recombinant S-adenosyl-L homocysteine hydrolase (EC 3.3.1.1). In sharp contrast to KOBut, when lithium azide was adopted as a base, 9-[(1'R,2'S,3'R)-2',3'-O-isopropylidened ioxy-4'-cyclopenten-1'-yl]-H-adenine was selectively obtained, and subsequent deprotection afforded DHCeA, which is a well-known potential antiviral agent. (C) 2001 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0040-4039(00)01978-x
• 作为产物：
  描述：

  N6-苯甲酰基腺嘌呤 在 四氧化锇 、 四(三苯基膦)钯 、 水 、 sodium hydride 、 N-甲基吗啉氧化物 、 三苯基膦 作用下， 以 四氢呋喃 、 二甲基亚砜 为溶剂， 反应 53.0h， 生成 N⁶-benzoylnoraristeromycin
  参考文献：
  名称：

  Synthesis of base-modified noraristeromycin derivatives and their inhibitory activity against human and Plasmodium falciparum recombinant S-adenosyl-l-homocysteine hydrolase

  摘要：

  Noraristeromycin derivatives possessing 2- or 8-position modified adenine or 8-aza-7-deazaadenine were synthesized, and their inhibitory activity against human and Plasmodium falciparum (P. falciparum) recombinant SAH hydrolases was investigated. Among these noraristeromycin derivatives, 2-aminonoraristeromycin selectively showed inhibitory activity against P. falciparum recombinant SAH hydrolase. (C) 2002 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0040-4020(01)01247-9

文献信息

• Facile synthesis of 9-[(1′R,2′S)-2′-hydroxy-3′-oxocyclopentan-1′-yl]-9-H-adenine possessing inhibitory activity against human recombinant S-adenosyl-l-homocysteine hydrolase
  作者：Yukio Kitade、Atushi Kozaki、Chizuko Yatome

  DOI：10.1016/s0040-4039(00)01978-x

  日期：2001.1

  Treatment of 4'-O-methanesulfonyl-2',3'-O-isopropylideneoraisteromycin with KOBut gave the corresponding 3',4'-dehydro derivative, and subsequent deprotection resulted in the formation of 9-[(1'R,2'S)-2'-hydroxy-3'-oxocyclopentan-1'-yl]-9-H-adenine possessing inhibitory activity against human recombinant S-adenosyl-L homocysteine hydrolase (EC 3.3.1.1). In sharp contrast to KOBut, when lithium azide was adopted as a base, 9-[(1'R,2'S,3'R)-2',3'-O-isopropylidened ioxy-4'-cyclopenten-1'-yl]-H-adenine was selectively obtained, and subsequent deprotection afforded DHCeA, which is a well-known potential antiviral agent. (C) 2001 Elsevier Science Ltd. All rights reserved.
• Synthesis of base-modified noraristeromycin derivatives and their inhibitory activity against human and Plasmodium falciparum recombinant S-adenosyl-l-homocysteine hydrolase
  作者：Yukio Kitade、Atushi Kozaki、Toshihiro Miwa、Masayuki Nakanishi

  DOI：10.1016/s0040-4020(01)01247-9

  日期：2002.2

  Noraristeromycin derivatives possessing 2- or 8-position modified adenine or 8-aza-7-deazaadenine were synthesized, and their inhibitory activity against human and Plasmodium falciparum (P. falciparum) recombinant SAH hydrolases was investigated. Among these noraristeromycin derivatives, 2-aminonoraristeromycin selectively showed inhibitory activity against P. falciparum recombinant SAH hydrolase. (C) 2002 Elsevier Science Ltd. All rights reserved.