HOC6H4CHN(i-Pr) | 13033-49-3

• 分子结构分类: 有机化合物 - 苯类化合物 - 酚类
• 英文名称: HOC6H4CHN(i-Pr)
• 英文别名: N-(m-Hydroxybenzyliden)-isopropylamin；3-(Propan-2-yliminomethyl)phenol
• CAS: 13033-49-3
• 化学式: C₁₀H₁₃NO
• 分子量: 163.219
• InChiKey: RJUYVYIKNIJHLS-UHFFFAOYSA-N

物化性质

• 沸点：
  288.7±23.0 °C(Predicted)
• 密度：
  0.98±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  2.3
• 重原子数：
  12
• 可旋转键数：
  2
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.3
• 拓扑面积：
  32.6
• 氢给体数：
  1
• 氢受体数：
  2

反应信息

• 作为反应物：
  描述：

  HOC6H4CHN(i-Pr) 在 sodium tetrahydroborate 作用下， 以 乙醇 、 甲苯 为溶剂， 反应 35.0h， 生成 3-[N-isopropyl-N-(3-hydroxybenzyl)amino]propoxyxanthen-9-one
  参考文献：
  名称：

  Acetylcholinesterase Inhibitors:  Synthesis and Structure−Activity Relationships of ω-[N-Methyl-N-(3-alkylcarbamoyloxyphenyl)- methyl]aminoalkoxyheteroaryl Derivatives

  摘要：

  Acetylcholinesterase (AChE) inhibitors are one of the most actively investigated classes of compounds in the search for an effective treatment of Alzheimer's disease. This work describes the synthesis, AChE inhibitory activity, and structure-activity relationships of some compounds related to a recently discovered series of AChE inhibitors: the omega-[N-methyl-N-(3-alkylcarbamoyloxyphenyl)methyl]aminoalkoxyxanthen-9-ones. The influence of structural variations on the inhibitory potency was carefully investigated by modifying different parts of the parent molecule, and a theoretical model of the binding of one representative compound to the enzyme was developed. The biological properties of the series were investigated in some detail by considering not only the activity on isolated enzyme but the selectivity with respect to butyrylcholinesterase (BuChE) and the in vitro inhibitory activity on rat cerebral cortex as well. Some of the newly synthesized derivatives, when tested on isolated and/or AChE-enriched rat brain cortex fraction, displayed a selective inhibitory activity and were more active than physostigmine. In particular, compound 13, an azaxanthone derivative, displayed the best rat cortex AChE inhibition (190-fold higher than physostigmine), as well as a high degree of enzyme selectivity (over 60-fold more selective for AChE than for BuChE). When tested in the isolated enzyme, compound 13 was less active, suggesting some differences either in drug availability/biotransformation or in the inhibitor-sensitive residues of the enzyme when biologically positioned in rat brain membranes.

  DOI：

  10.1021/jm9810046
• 作为产物：
  描述：

  间羟基苯甲醛 、 异丙胺 在 magnesium sulfate 作用下， 以 二氯甲烷 为溶剂， 反应 3.0h， 生成 HOC6H4CHN(i-Pr)
  参考文献：
  名称：

  Kuwano, Eiichi; Hisano, Tomomi; Eto, Morifusa, Agricultural and Biological Chemistry, 1991, vol. 55, # 12, p. 2999 - 3004

  摘要：

  DOI：

文献信息

• Facile synthesis of achiral and chiral PCN pincer palladium(II) complexes and their application in the Suzuki and copper-free Sonogashira cross-coupling reactions
  作者：Ben-Shang Zhang、Chao Wang、Jun-Fang Gong、Mao-Ping Song

  DOI：10.1016/j.jorganchem.2009.04.002

  日期：2009.7

  Five non-symmetrical PCN pincer palladium(II) complexes [PdClC6H3-2-(CH=NR)-6-(OPR'(2))}] (R = m-ClC6H4, R' = Ph (2a); R = Ph, R' = Ph (2b); R = i-Pr, R' = Ph (2c); R = m-ClC6H4, R' = i-Pr (2d); R = (S)-1-phenylethyl, R' = Ph (2e)) have been easily prepared in only two steps from readily available m-hydroxybenzaldehyde and characterized by HRMS, H-1 NMR, C-13 NMR, P-31 NMR and IR spectra. The molecular structures of 2a and 2b have been further determined by X-ray single-crystal diffraction. The obtained Pd complexes were found to be effective catalysts for the Suzuki and copper-free Sonogashira cross-coupling reactions which could be carried out in the undried solvent under air. (C) 2009 Elsevier B.V. All rights reserved.
• Kuwano, Eiichi; Hisano, Tomomi; Eto, Morifusa, Agricultural and Biological Chemistry, 1991, vol. 55, # 12, p. 2999 - 3004
  作者：Kuwano, Eiichi、Hisano, Tomomi、Eto, Morifusa

  DOI：——

  日期：——
• Acetylcholinesterase Inhibitors:  Synthesis and Structure−Activity Relationships of ω-[<i>N</i>-Methyl-<i>N</i>-(3-alkylcarbamoyloxyphenyl)- methyl]aminoalkoxyheteroaryl Derivatives
  作者：Angela Rampa、Alessandra Bisi、Piero Valenti、Maurizio Recanatini、Andrea Cavalli、Vincenza Andrisano、Vanni Cavrini、Lorena Fin、Alessandro Buriani、Pietro Giusti

  DOI：10.1021/jm9810046

  日期：1998.10.1

  Acetylcholinesterase (AChE) inhibitors are one of the most actively investigated classes of compounds in the search for an effective treatment of Alzheimer's disease. This work describes the synthesis, AChE inhibitory activity, and structure-activity relationships of some compounds related to a recently discovered series of AChE inhibitors: the omega-[N-methyl-N-(3-alkylcarbamoyloxyphenyl)methyl]aminoalkoxyxanthen-9-ones. The influence of structural variations on the inhibitory potency was carefully investigated by modifying different parts of the parent molecule, and a theoretical model of the binding of one representative compound to the enzyme was developed. The biological properties of the series were investigated in some detail by considering not only the activity on isolated enzyme but the selectivity with respect to butyrylcholinesterase (BuChE) and the in vitro inhibitory activity on rat cerebral cortex as well. Some of the newly synthesized derivatives, when tested on isolated and/or AChE-enriched rat brain cortex fraction, displayed a selective inhibitory activity and were more active than physostigmine. In particular, compound 13, an azaxanthone derivative, displayed the best rat cortex AChE inhibition (190-fold higher than physostigmine), as well as a high degree of enzyme selectivity (over 60-fold more selective for AChE than for BuChE). When tested in the isolated enzyme, compound 13 was less active, suggesting some differences either in drug availability/biotransformation or in the inhibitor-sensitive residues of the enzyme when biologically positioned in rat brain membranes.