hex-5-ynyl 4-nitrophenyl hexylphosphonate | 1306635-46-0

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: hex-5-ynyl 4-nitrophenyl hexylphosphonate
• 英文别名: Hex-5-ynyl 4-nitrophenyl hexylphosphonate；1-[hexyl(hex-5-ynoxy)phosphoryl]oxy-4-nitrobenzene
• CAS: 1306635-46-0
• 化学式: C₁₈H₂₆NO₅P
• 分子量: 367.382
• InChiKey: NVVJBHLSFDGOSU-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.6
• 重原子数：
  25
• 可旋转键数：
  12
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.56
• 拓扑面积：
  81.4
• 氢给体数：
  0
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  hex-5-ynyl 4-nitrophenyl hexylphosphonate 在 fluoride on polymer 作用下， 以 乙腈 为溶剂， 以100%的产率得到
  参考文献：
  名称：

  按需氟膦酸盐：氟膦酸盐合成的通用和简化方法

  摘要：

  要求不高：已开发出一种稳健且无需纯化的一步合成方法，能够从稳定且可储存的对硝基苯基膦酸盐的稳定“工具箱”中按需制备结构多样的氟膦酸盐。此外，还强调了反应检测方案，进一步促进了这些有价值的基于活性的探针的快速筛选。

  DOI：

  10.1002/cbic.202000852
• 作为产物：
  描述：

  对硝基苯酚 、 hex-5-yn-1-yl hexylphosphonochloridate 在 四氮唑 、 N,N-二异丙基乙胺 作用下， 以 二氯甲烷 、 乙腈 为溶剂， 反应 16.0h， 生成 hex-5-ynyl 4-nitrophenyl hexylphosphonate
  参考文献：
  名称：

  Activity based subcellular resolution imaging of lipases

  摘要：

  Lipases play a key role in whole body energy homeostasis. Dysregulation of lipolytic activities affects lipid absorption, mobilization, and transport, and is causative for lipid-related diseases. Regulation of enzymes involved in lipid metabolism is governed by a complex network of protein-protein and protein-small molecule interactions. Thus these enzymes have to be studied under the physiologically most relevant conditions, that is, in vivo. Our latest generation of activity based probes designed for capturing of lipases employs bioorthogonal chemical linker groups, which are membrane permeable and thus allow studying protein activity in living cells. Another advantage is the virtually unlimited choice of reporter tags. Here we report on a novel method combining in vivo activity based labeling of lipases with in situ detection of lipolytic activities by on slide click chemistry and imaging by fluorescence microscopy. We demonstrate that cytosolic as well as organelle resident lipases are specifically labeled in intact living cells. This method will shed light on the (sub)cellular localization of lipolytic proteomes of cells and tissues in health and disease directly at enzymatic activity level without the need of prior knowledge of the identities of the responsible enzymes or dependence on the availability of specific antibodies. (C) 2011 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2011.04.018

文献信息

• Fluorophosphonates on‐Demand: A General and Simplified Approach toward Fluorophosphonate Synthesis
  作者：Jason K. Dutra、Timothy L. Foley、Zhen Huang、Ethan L. Fisher、Erik A. Lachapelle、Subham Mahapatra、Kevin Ogilvie、Todd W. Butler、Justin Bellenger、Jaimeen Devraj Majmudar、Christopher W. am Ende

  DOI：10.1002/cbic.202000852

  日期：2021.5.14

  Not too demanding: A robust and purification-free, one-step synthesis has been developed to enable the on-demand preparation of structurally diverse fluorophosphonates from a stable, and storable “toolbox” of readily accessible p-nitrophenylphosphonates. Additionally, a reaction-to-assay protocol is highlighted that further facilitates the rapid screening of these valuable activity-based probes.

  要求不高：已开发出一种稳健且无需纯化的一步合成方法，能够从稳定且可储存的对硝基苯基膦酸盐的稳定“工具箱”中按需制备结构多样的氟膦酸盐。此外，还强调了反应检测方案，进一步促进了这些有价值的基于活性的探针的快速筛选。
• Activity based subcellular resolution imaging of lipases
  作者：Martin Viertler、Matthias Schittmayer、Ruth Birner-Gruenberger

  DOI：10.1016/j.bmc.2011.04.018

  日期：2012.1

  Lipases play a key role in whole body energy homeostasis. Dysregulation of lipolytic activities affects lipid absorption, mobilization, and transport, and is causative for lipid-related diseases. Regulation of enzymes involved in lipid metabolism is governed by a complex network of protein-protein and protein-small molecule interactions. Thus these enzymes have to be studied under the physiologically most relevant conditions, that is, in vivo. Our latest generation of activity based probes designed for capturing of lipases employs bioorthogonal chemical linker groups, which are membrane permeable and thus allow studying protein activity in living cells. Another advantage is the virtually unlimited choice of reporter tags. Here we report on a novel method combining in vivo activity based labeling of lipases with in situ detection of lipolytic activities by on slide click chemistry and imaging by fluorescence microscopy. We demonstrate that cytosolic as well as organelle resident lipases are specifically labeled in intact living cells. This method will shed light on the (sub)cellular localization of lipolytic proteomes of cells and tissues in health and disease directly at enzymatic activity level without the need of prior knowledge of the identities of the responsible enzymes or dependence on the availability of specific antibodies. (C) 2011 Elsevier Ltd. All rights reserved.