1,1'-bis(pyridinium)-naphthyl-3,6-dimethylene dibromide | 114003-26-8

• 分子结构分类: 有机化合物 - 苯类化合物 - 萘
• 英文名称: 1,1'-bis(pyridinium)-naphthyl-3,6-dimethylene dibromide
• 英文别名: 2,7-bis-pyridiniomethyl-naphthalene; dibromide；2,7-Bis-pyridiniomethyl-naphthalin; Dibromid
• CAS: 114003-26-8
• 化学式: 2Br*C₂₂H₂₀N₂
• 分子量: 472.222
• InChiKey: XYADRPFLECDRLT-UHFFFAOYSA-M

计算性质

• 辛醇/水分配系数(LogP)：
  0.52
• 重原子数：
  25.0
• 可旋转键数：
  4.0
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.09
• 拓扑面积：
  7.76
• 氢给体数：
  0.0
• 氢受体数：
  0.0

反应信息

• 作为产物：
  描述：

  吡啶 、 2,7-双(溴甲基)萘 在 乙醇 作用下， 生成 1,1'-bis(pyridinium)-naphthyl-3,6-dimethylene dibromide
  参考文献：
  名称：

  Ried et al., Chemische Berichte, 1958, vol. 91, p. 2472,2477

  摘要：

  DOI：

文献信息

• Preparation and in vitro screening of symmetrical bispyridinium cholinesterase inhibitors bearing different connecting linkage—initial study for Myasthenia gravis implications
  作者：Kamil Musilek、Marketa Komloova、Vlasta Zavadova、Ondrej Holas、Martina Hrabinova、Miroslav Pohanka、Vlastimil Dohnal、Florian Nachon、Martin Dolezal、Kamil Kuca、Young-Sik Jung

  DOI：10.1016/j.bmcl.2010.01.034

  日期：2010.3

  Reversible inhibitors (e. g., pyridostigmine bromide, neostigmine bromide) of carbamate origin are used in the early treatment of Myasthenia gravis (MG) to block acetylcholinesterase (AChE) native function and conserve efficient amount of acetylcholine for decreasing number of nicotinic receptors. Carbamate inhibitors are known for many undesirable side effects related to the reversible inhibition of AChE. In contrast, this paper describes 20 newly prepared bispyridinium inhibitors of potential concern for MG. Although some compounds from this series have been known before, they were not assayed for cholinesterase inhibition yet.The newly prepared compounds were evaluated in vitro on human erythrocyte AChE and human plasmatic butyrylcholinesterase (BChE). Their inhibitory ability was expressed as IC(50) and compared to standard carbamate drugs. Three compounds presented promising inhibition (in mu M range) of both enzymes in vitro similar to the used standards. The novel inhibitors did not present selectivity between AChE and BChE. Two newly prepared compounds were chosen for docking studies and confirmed apparent pi-pi or pi-cationic interactions aside enzyme's catalytic sites. The kinetics assay confirmed non-competitive inhibition of AChE by two best newly prepared compounds. (C) 2010 Elsevier Ltd. All rights reserved.