4-(1H-imidazol-1-yl)phenylmethyl bromide hydrobromide

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 唑类
• 英文名称: 4-(1H-imidazol-1-yl)phenylmethyl bromide hydrobromide
• 英文别名: 1-(4-(Bromomethyl)phenyl)-1H-imidazole hydrobromide；1-[4-(bromomethyl)phenyl]imidazole;hydrobromide
• 化学式: BrH*C₁₀H₉BrN₂
• 分子量: 318.011
• InChiKey: IYCDHZJWPOCAFN-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.35
• 重原子数：
  14
• 可旋转键数：
  2
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.1
• 拓扑面积：
  17.8
• 氢给体数：
  1
• 氢受体数：
  1

反应信息

• 作为反应物：
  描述：

  4-(1H-imidazol-1-yl)phenylmethyl bromide hydrobromide 在 盐酸 、 硫酸 作用下， 以 乙腈 为溶剂， 反应 51.0h， 生成 ethyl 4-(1-imidazolyl)phenylacetate
  参考文献：
  名称：

  Aromatic hydrazides as specific inhibitors of bovine serum amine oxidase

  摘要：

  New hydrazides were synthesized in search for specific inhibitors of bovine serum amine oxidase: a series of benzoic and phenylacetic acid hydrazides containing the 1H-imidazol-1-yl or the 1H-imidazol-1-ylmethyl group as (o, m, p)-substituent in the phenyl ring; an analogous series of p-substituted phenylhydrazides with 5 or 6-membered heterocyclic ring as substituent, and a series of similar phenylpropionic hydrazides. The longer and more flexible phenylacetic hydrazides, and to a somewhat lesser extent the phenylpropionic ones, were better specific inhibitors of bovine serum amine oxidase than the benzoic hydrazides, which were also bound by the enzyme with high affinity, but at a slow rate. Derivatives with p- and m -substituents were more reactive than the o-substituted ones. The chemical nature of the substituent was less important than its position in the phenyl ring and the presence of methylene spacers. These data point to the presence of a hydrophobic site at short distance from the protein carbonyl cofactor, so that simultaneous interaction of the 2 ends of the inhibitor molecule can occur at the 2 sites. The presence of the hydrophobic site was confirmed by the capability of some molecule deprived of the hydrazidic group to act as mild inhibitors. All hydrazides were less reactive by 2-3 orders of magnitude towards pig kidney diamine oxidase and FAD-dependent monoamine oxidase from rat brain mitochondria, while the other compounds showed similar inhibition power against all proteins. The specificity for the bovine enzyme seems therefore to be related to the concerted action of the 2 moieties of the inhibitor molecule.

  DOI：

  10.1016/0223-5234(92)90005-l
• 作为产物：
  描述：

  4-(1-咪唑基)苄醇 在 氢溴酸 作用下， 以 水 为溶剂， 以79%的产率得到4-(1H-imidazol-1-yl)phenylmethyl bromide hydrobromide
  参考文献：
  名称：

  Aromatic hydrazides as specific inhibitors of bovine serum amine oxidase

  摘要：

  New hydrazides were synthesized in search for specific inhibitors of bovine serum amine oxidase: a series of benzoic and phenylacetic acid hydrazides containing the 1H-imidazol-1-yl or the 1H-imidazol-1-ylmethyl group as (o, m, p)-substituent in the phenyl ring; an analogous series of p-substituted phenylhydrazides with 5 or 6-membered heterocyclic ring as substituent, and a series of similar phenylpropionic hydrazides. The longer and more flexible phenylacetic hydrazides, and to a somewhat lesser extent the phenylpropionic ones, were better specific inhibitors of bovine serum amine oxidase than the benzoic hydrazides, which were also bound by the enzyme with high affinity, but at a slow rate. Derivatives with p- and m -substituents were more reactive than the o-substituted ones. The chemical nature of the substituent was less important than its position in the phenyl ring and the presence of methylene spacers. These data point to the presence of a hydrophobic site at short distance from the protein carbonyl cofactor, so that simultaneous interaction of the 2 ends of the inhibitor molecule can occur at the 2 sites. The presence of the hydrophobic site was confirmed by the capability of some molecule deprived of the hydrazidic group to act as mild inhibitors. All hydrazides were less reactive by 2-3 orders of magnitude towards pig kidney diamine oxidase and FAD-dependent monoamine oxidase from rat brain mitochondria, while the other compounds showed similar inhibition power against all proteins. The specificity for the bovine enzyme seems therefore to be related to the concerted action of the 2 moieties of the inhibitor molecule.

  DOI：

  10.1016/0223-5234(92)90005-l

文献信息

• Aromatic hydrazides as specific inhibitors of bovine serum amine oxidase
  作者：M Artico、R Silvestri、G Stefancich、L Avigliano、A Di Giulio、M Maccarrone、E Agostinelli、B Mondovi、L Morpurgo

  DOI：10.1016/0223-5234(92)90005-l

  日期：1992.4

  New hydrazides were synthesized in search for specific inhibitors of bovine serum amine oxidase: a series of benzoic and phenylacetic acid hydrazides containing the 1H-imidazol-1-yl or the 1H-imidazol-1-ylmethyl group as (o, m, p)-substituent in the phenyl ring; an analogous series of p-substituted phenylhydrazides with 5 or 6-membered heterocyclic ring as substituent, and a series of similar phenylpropionic hydrazides. The longer and more flexible phenylacetic hydrazides, and to a somewhat lesser extent the phenylpropionic ones, were better specific inhibitors of bovine serum amine oxidase than the benzoic hydrazides, which were also bound by the enzyme with high affinity, but at a slow rate. Derivatives with p- and m -substituents were more reactive than the o-substituted ones. The chemical nature of the substituent was less important than its position in the phenyl ring and the presence of methylene spacers. These data point to the presence of a hydrophobic site at short distance from the protein carbonyl cofactor, so that simultaneous interaction of the 2 ends of the inhibitor molecule can occur at the 2 sites. The presence of the hydrophobic site was confirmed by the capability of some molecule deprived of the hydrazidic group to act as mild inhibitors. All hydrazides were less reactive by 2-3 orders of magnitude towards pig kidney diamine oxidase and FAD-dependent monoamine oxidase from rat brain mitochondria, while the other compounds showed similar inhibition power against all proteins. The specificity for the bovine enzyme seems therefore to be related to the concerted action of the 2 moieties of the inhibitor molecule.