5'-O-pentyloxycarbonyladenosine

• 分子结构分类: 有机化合物 - 核苷、核苷酸和类似物 - 嘌呤核苷
• 英文名称: 5'-O-pentyloxycarbonyladenosine
• 英文别名: [(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methyl pentyl carbonate
• 化学式: C₁₆H₂₃N₅O₆
• 分子量: 381.389
• InChiKey: CJHLVDSPXNTHQJ-SDBHATRESA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.2
• 重原子数：
  27
• 可旋转键数：
  9
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.62
• 拓扑面积：
  155
• 氢给体数：
  3
• 氢受体数：
  10

反应信息

• 作为产物：
  描述：

  2',3'-O-isopropylidene-5'-O-pentyloxycarbonyladenosine 在 甲酸 作用下， 以 水 为溶剂， 反应 24.0h， 以88%的产率得到5'-O-pentyloxycarbonyladenosine
  参考文献：
  名称：

  Identification of 8-Aminoadenosine Derivatives as a New Class of Human Concentrative Nucleoside Transporter 2 Inhibitors

  摘要：

  Purine-rich foods have long been suspected as a major cause of hyperuricemia. We hypothesized that inhibition of human concentrative nucleoside transporter 2 (hCNT2) would suppress increases in serum urate levels derived from dietary purines. To test this hypothesis, the development of potent hCNT2 inhibitors was required. By modifying adenosine, an hCNT2 substrate, we successfully identified 8-aminoadenosine derivatives as a new class of hCNT2 inhibitors. Compound 12 moderately inhibited hCNT2 (IC50 = 52 +/- 3.8 mu M), and subsequent structure-activity relationship studies led to the discovery of compound 48 (IC50 = 0.64 +/- 0.19 mu M). Here we describe significant findings about structural requirements of 8-aminoadenosine derivatives for exhibiting potent hCNT2 inhibitory activity.

  DOI：

  10.1021/ml500343r

文献信息

• Identification of 8-Aminoadenosine Derivatives as a New Class of Human Concentrative Nucleoside Transporter 2 Inhibitors
  作者：Kazuya Tatani、Masahiro Hiratochi、Yoshinori Nonaka、Masayuki Isaji、Satoshi Shuto

  DOI：10.1021/ml500343r

  日期：2015.3.12

  Purine-rich foods have long been suspected as a major cause of hyperuricemia. We hypothesized that inhibition of human concentrative nucleoside transporter 2 (hCNT2) would suppress increases in serum urate levels derived from dietary purines. To test this hypothesis, the development of potent hCNT2 inhibitors was required. By modifying adenosine, an hCNT2 substrate, we successfully identified 8-aminoadenosine derivatives as a new class of hCNT2 inhibitors. Compound 12 moderately inhibited hCNT2 (IC50 = 52 +/- 3.8 mu M), and subsequent structure-activity relationship studies led to the discovery of compound 48 (IC50 = 0.64 +/- 0.19 mu M). Here we describe significant findings about structural requirements of 8-aminoadenosine derivatives for exhibiting potent hCNT2 inhibitory activity.