4-hydrazino-N-hexyl-1,8-naphthalimide | 1000622-37-6

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 异喹啉及其衍生物
• 英文名称: 4-hydrazino-N-hexyl-1,8-naphthalimide
• 英文别名: 2-hexyl-6-hydrazino-1H-benzo[de]isoquinoline-1,3(2H)-dione；2-hexyl-6-hydrazinylbenzo[de]isoquinoline-1,3-dione
• CAS: 1000622-37-6
• 化学式: C₁₈H₂₁N₃O₂
• 分子量: 311.384
• InChiKey: JBAFTOWXTDAYGS-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.7
• 重原子数：
  23
• 可旋转键数：
  6
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.33
• 拓扑面积：
  75.4
• 氢给体数：
  2
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  Boc-L-蛋氨酸 、 4-hydrazino-N-hexyl-1,8-naphthalimide 在 N-[(1H-benzotriazol-1-yl)(dimethylamino)methylene]-N-methylmethanaminium tetrafluoroborate 、 1-羟基苯并三唑 、 N,N-二异丙基乙胺 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 1.0h， 以81%的产率得到N-tert-butoxycarbonyl-L-methionine N'-(2-hexyl-1,3-dioxo-2,3-dihydro-1H-benzo[de]isoquinolin-6-yl)hydrazide
  参考文献：
  名称：

  Synthesis and use of 4-peptidylhydrazido-N-hexyl-1,8-naphthalimides as fluorogenic histochemical substrates for dipeptidyl peptidase IV and tripeptidyl peptidase I

  摘要：

  Gly-Pro-, Gly-Pro-Met- and Ala-Ala-Phe-N'-(2-hexyl-1,3-dioxo-2,3-dihydro-1H-benzo[de]isoquinolin-6-yl)-hydrazides are synthesized by guanidinium/uronium type condensing reagent and used as fluorogenic substrates to localize dipeptidyl peptidase IV and tripeptidyl peptidase I activities in mammalian tissue sections. Enzyme hydrolysis releases 2-hexyl-6-hydrazino-1H-benzo[de]isoquinoline-1,3(2H)-dione, which couples with piperonal to form insoluble fluorescent hydrazone, precipitating on the enzyme locations and marking them. The fluorescent technique reveals precisely the enzymes locations at the lack of background noise in a single incubation step. It avoids most of the drawbacks of the previously proposed fluorescent histochemical techniques and can be valuable for the in situ studies of these enzymes in norm and pathology. (C) 2008 Elsevier Masson SAS. All rights reserved.

  DOI：

  10.1016/j.ejmech.2008.02.036
• 作为产物：
  描述：

  4-chloro-N-hexyl-1,8-naphthalimide 在 一水合肼 作用下， 以 二甲基亚砜 为溶剂， 反应 4.0h， 以43%的产率得到4-hydrazino-N-hexyl-1,8-naphthalimide
  参考文献：
  名称：

  Synthesis and use of 4-peptidylhydrazido-N-hexyl-1,8-naphthalimides as fluorogenic histochemical substrates for dipeptidyl peptidase IV and tripeptidyl peptidase I

  摘要：

  Gly-Pro-, Gly-Pro-Met- and Ala-Ala-Phe-N'-(2-hexyl-1,3-dioxo-2,3-dihydro-1H-benzo[de]isoquinolin-6-yl)-hydrazides are synthesized by guanidinium/uronium type condensing reagent and used as fluorogenic substrates to localize dipeptidyl peptidase IV and tripeptidyl peptidase I activities in mammalian tissue sections. Enzyme hydrolysis releases 2-hexyl-6-hydrazino-1H-benzo[de]isoquinoline-1,3(2H)-dione, which couples with piperonal to form insoluble fluorescent hydrazone, precipitating on the enzyme locations and marking them. The fluorescent technique reveals precisely the enzymes locations at the lack of background noise in a single incubation step. It avoids most of the drawbacks of the previously proposed fluorescent histochemical techniques and can be valuable for the in situ studies of these enzymes in norm and pathology. (C) 2008 Elsevier Masson SAS. All rights reserved.

  DOI：

  10.1016/j.ejmech.2008.02.036

文献信息

• 10.1021/acs.jmedchem.4c00209
  作者：Wang, Jin-Xin、Zhang, Peng-Li、Gopala, Lavanya、Lv, Jing-Song、Lin, Jian-Mei、Zhou, Cheng-He

  DOI：10.1021/acs.jmedchem.4c00209

  日期：——

  This study developed a class of novel structural antifungal hydrazylnaphthalimidols (HNs) with multitargeting broad-spectrum potential via multicomponent hybridization to confront increasingly severe fungal invasion. Some prepared HNs exhibited considerable antifungal potency; especially nitrofuryl HN 4a (MIC = 0.001 mM) exhibited a potent antifungal activity against Candida albicans, which is 13-fold

  这项研究通过多组分杂交开发了一类新型结构抗真菌肼基萘甲酰亚胺（HN），具有多靶点广谱潜力，可应对日益严重的真菌入侵。一些制备的 HN 表现出相当大的抗真菌效力；尤其是硝基呋喃 HN 4a (MIC = 0.001 mM) 对白色念珠菌表现出有效的抗真菌活性，比氟康唑高 13 倍。此外，硝基呋喃 HN 4a具有低细胞毒性、溶血性和抗性，以及快速的杀菌功效。初步机制研究表明，硝基呋喃 HN 4a可以抑制乳酸脱氢酶，从而降低代谢活性并促进活性氧的积累，从而导致氧化应激。此外，硝基呋喃 HN 4a没有表现出膜靶向能力；它可以嵌入DNA以阻止DNA复制，但不能切割DNA。这些发现表明，HN 有希望作为治疗真菌感染的潜在多靶点广谱抗真菌候选物的新型结构支架。
• Synthesis, structural analysis and application of a series of solid-state fluorochromes—aryl hydrazones of 4-hydrazino-N-hexyl-1,8-naphthalimide
  作者：Ivaylo P. Ivanov、Mashenka B. Dimitrova、Donka N. Tasheva、Diana V. Cheshmedzhieva、Valentin S. Lozanov、Sonia V. Ilieva

  DOI：10.1016/j.tet.2012.10.093

  日期：2013.1

  The development of red solid-state fluorochromes is important for different applications. The influence of the electronic effects of substituents on the chemical shifts in the H-1 NMR spectra and solid-state fluorescent properties of aryl hydrazones of 4-hydrazino-N-hexyl-1,8-naphthalimide is evaluated. The main fragmentation pathway of hydrazones is determined using electrospray ionization mass spectrometry and high resolution MS/MS. A possible application of these fluorochromes for the in situ imaging of enzyme activities is presented. (c) 2012 Elsevier Ltd. All rights reserved.
• Synthesis and use of 4-peptidylhydrazido-N-hexyl-1,8-naphthalimides as fluorogenic histochemical substrates for dipeptidyl peptidase IV and tripeptidyl peptidase I
  作者：Ivaylo Ivanov、Donka Tasheva、Ralitza Todorova、Mashenka Dimitrova

  DOI：10.1016/j.ejmech.2008.02.036

  日期：2009.1

  Gly-Pro-, Gly-Pro-Met- and Ala-Ala-Phe-N'-(2-hexyl-1,3-dioxo-2,3-dihydro-1H-benzo[de]isoquinolin-6-yl)-hydrazides are synthesized by guanidinium/uronium type condensing reagent and used as fluorogenic substrates to localize dipeptidyl peptidase IV and tripeptidyl peptidase I activities in mammalian tissue sections. Enzyme hydrolysis releases 2-hexyl-6-hydrazino-1H-benzo[de]isoquinoline-1,3(2H)-dione, which couples with piperonal to form insoluble fluorescent hydrazone, precipitating on the enzyme locations and marking them. The fluorescent technique reveals precisely the enzymes locations at the lack of background noise in a single incubation step. It avoids most of the drawbacks of the previously proposed fluorescent histochemical techniques and can be valuable for the in situ studies of these enzymes in norm and pathology. (C) 2008 Elsevier Masson SAS. All rights reserved.