9-O-[3-(benzotriazol-1-yloxy)propyl]berberine bromide | 1219819-20-1

• 分子结构分类: 有机化合物 - 生物碱及其衍生物 - 原小檗碱生物碱及其衍生物
• 英文名称: 9-O-[3-(benzotriazol-1-yloxy)propyl]berberine bromide
• 英文别名: 16-[3-(Benzotriazol-1-yloxy)propoxy]-17-methoxy-5,7-dioxa-13-azoniapentacyclo[11.8.0.02,10.04,8.015,20]henicosa-1(13),2,4(8),9,14,16,18,20-octaene;bromide
• CAS: 1219819-20-1
• 化学式: Br*C₂₈H₂₅N₄O₅
• 分子量: 577.434
• InChiKey: CNYNXTDEJYBPOF-UHFFFAOYSA-M

计算性质

• 辛醇/水分配系数(LogP)：
  0.73
• 重原子数：
  38
• 可旋转键数：
  7
• 环数：
  7.0
• sp3杂化的碳原子比例：
  0.25
• 拓扑面积：
  80.7
• 氢给体数：
  0
• 氢受体数：
  8

反应信息

• 作为产物：
  描述：

  1-(3-bromopropoxy)-benzotriazole 、 berberrubine 在 potassium carbonate 作用下， 以 乙腈 为溶剂， 以66%的产率得到9-O-[3-(benzotriazol-1-yloxy)propyl]berberine bromide
  参考文献：
  名称：

  Synthesis, biological evaluation, and molecular modeling of berberine derivatives as potent acetylcholinesterase inhibitors

  摘要：

  By targeting the dual active sites of acetylcholinesterase (AChE), a new series of berberine derivatives was designed, synthesized, and evaluated as AChE inhibitors. Most of the derivatives inhibited AChE in the sub-micromolar range. Compound 8c, berberine linked with phenol by a 4-carbon spacer, showed the most potent inhibition of AChE. A kinetic study of AChE and BuChE indicated that a mix-competitive binding mode existed for these berberine derivatives. Molecular modeling studies confirmed that these hybrids target both the catalytic active site (CAS) and the peripheral anionic site (PAS) of AChE. This is the first report where AChE inhibitory activity has been associated with berberine as a lead molecule. (C) 2009 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2009.12.035

文献信息

• Synthesis, biological evaluation, and molecular modeling of berberine derivatives as potent acetylcholinesterase inhibitors
  作者：Ling Huang、Anding Shi、Feng He、Xingshu Li

  DOI：10.1016/j.bmc.2009.12.035

  日期：2010.2

  By targeting the dual active sites of acetylcholinesterase (AChE), a new series of berberine derivatives was designed, synthesized, and evaluated as AChE inhibitors. Most of the derivatives inhibited AChE in the sub-micromolar range. Compound 8c, berberine linked with phenol by a 4-carbon spacer, showed the most potent inhibition of AChE. A kinetic study of AChE and BuChE indicated that a mix-competitive binding mode existed for these berberine derivatives. Molecular modeling studies confirmed that these hybrids target both the catalytic active site (CAS) and the peripheral anionic site (PAS) of AChE. This is the first report where AChE inhibitory activity has been associated with berberine as a lead molecule. (C) 2009 Elsevier Ltd. All rights reserved.