2-[[N-(2-trimethylsilyl)ethoxycarbonyl]amino]ethanol | 162406-69-1

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: 2-[[N-(2-trimethylsilyl)ethoxycarbonyl]amino]ethanol
• 英文别名: 2-trimethylsilylethyl N-(2-hydroxyethyl)carbamate
• CAS: 162406-69-1
• 化学式: C₈H₁₉NO₃Si
• 分子量: 205.329
• InChiKey: UVDARLKWYSGJGS-UHFFFAOYSA-N

物化性质

• 沸点：
  298.3±25.0 °C(Predicted)
• 密度：
  0.996±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  1.04
• 重原子数：
  13
• 可旋转键数：
  6
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.88
• 拓扑面积：
  58.6
• 氢给体数：
  2
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  磷酸三(2,2,2-三氟乙基)酯 、 2-[[N-(2-trimethylsilyl)ethoxycarbonyl]amino]ethanol 在 1,8-二氮杂双环[5.4.0]十一碳-7-烯 作用下， 以 甲苯 为溶剂， 以90%的产率得到
  参考文献：
  名称：

  リン酸エステルの新規合成法

  摘要：

  在塩基性反應促進劑存在下，將三氟乙基磷酸三酯和醇反應的方法，用於高效製備磷酸三酯。

  公开号：

  JP2020183374A
• 作为产物：
  描述：

  对硝基苯基三甲基硅乙基碳酸酯 、 C.I.酸性橙108 在 三乙胺 作用下， 以 二氯甲烷 为溶剂， 以92%的产率得到2-[[N-(2-trimethylsilyl)ethoxycarbonyl]amino]ethanol
  参考文献：
  名称：

  Solid-Phase Synthesis of Polyamine Toxin Analogues:  Potent and Selective Antagonists of Ca²⁺-Permeable AMPA Receptors

  摘要：

  The wasp toxin philanthotoxin-433 (PhTX-433) is a nonselective and noncompetitive antagonist of ionotropic receptors, such as ionotropic glutamate receptors and nicotinic acetylcholine receptors. Polyamine toxins are extensively used for the characterization of subtypes of ionotropic glutamate receptors, in particular Ca2+-permeable AMPA and kainate receptors. We have previously shown that an analogue of PhTX-433 with one of the amino groups replaced by a methylene group, philanthotoxin-83 (PhTX-83) is a selective and potent antagonist of AMPA receptors. We now describe the solid-phase synthesis of analogues of PhTX-83 and the electrophysiological characterization of these analogues on cloned AMPA and kainate receptors. The polyamine portion of PhTX-83 was modified systematically by chaniging the position. of the. secondary amino group along the polyamine chain. In another series of analogues, the acyl moiety of PhTX-83 was replaced by acids of different size and lipophilicity. Using electrophysiological techniques, PhTX-56 was shown to be a highly potent (K-i = 3.3 +/- 0.78 nM) and voltage-dependent antagonist of homomeric GluR1 receptors and was more than 1000-fold less potent when tested on heteromeric GluR1+GluR2, as well as homomeric GluR5(Q) receptors, thus being selective for Ca2+-permeable AMPA receptors. Variation of the acyl group of PhTX-83 had only minor effect on antagonist potency at homomeric GluR receptors but led to a significant decrease in the voltage-dependence. In conclusion, PhTX-56 is a novel, very potent, and selective antagonist of Ca2+-permeable AMPA receptors and is a promising tool for structure/function studies of the ion channel of the AMPA receptor.

  DOI：

  10.1021/jm020314s

文献信息

• Amide compound libraries
  申请人：ISIS Pharmaceuticals, Inc.

  公开号：US06359061B1

  公开（公告）日：2002-03-19

  Amide compounds of formula (I), combinatorial libraries of amide compounds and methods of preparing the same are provided. Libraries of the invention are useful for screening in biological assays in order to identify pharmaceutically useful compounds.

  提供了公式（I）的酰胺化合物、酰胺化合物的组合库以及其制备方法。本发明的库可用于生物测定中的筛选，以便鉴定具有药用价值的化合物。
• EP3450435
  申请人：——

  公开号：——

  公开（公告）日：——
• Uncompetitive Antagonism of AMPA Receptors:  Mechanistic Insights from Studies of Polyamine Toxin Derivatives
  作者：Trine F. Andersen、Denis B. Tikhonov、Ulrik Bølcho、Konstantin Bolshakov、Jared K. Nelson、Florentina Pluteanu、Ian R. Mellor、Jan Egebjerg、Kristian Strømgaard

  DOI：10.1021/jm060606j

  日期：2006.9.1

  Philanthotoxins are uncompetitive antagonists of Ca2+-permeable AMPA receptors presumed to bind to the pore-forming region, but a detailed molecular mechanism for this interaction is missing. Here a small library of novel philanthotoxins was designed and synthesized using a solid-phase strategy. The biological activities were investigated at cloned and "native" AMPA receptors using electrophysiological techniques. A distinct relationship between length of the polyamine moiety and the location of a secondary amino group was observed. Fitting the data to the Woodhull equation allowed the first experimental demonstration of the relative location and orientation of the philanthotoxin molecule in the receptor. These results were corroborated by in silico studies using a homology model of the AMPA receptor ion channel. Together these studies provide strong evidence for a molecular mechanism by which polyamine toxins antagonize the AMPA receptor ion channel and provide the basis for rational development of uncompetitive antagonists of AMPA receptors.
• リン酸エステルの新規合成法
  申请人：株式会社 レオロジー機能食品研究所

  公开号：JP2020183374A

  公开（公告）日：2020-11-12

  【課題】目的とするリン酸トリエステルを効率的に製造する方法を提供すること。【解決手段】塩基性反応促進剤の存在下、リン酸トリス（２，２，２−トリフルオロエチル）とアルコールとを反応させることを特徴とするリン酸トリエステルの製造方法である。【選択図】なし

  在塩基性反應促進劑存在下，將三氟乙基磷酸三酯和醇反應的方法，用於高效製備磷酸三酯。
• Solid-Phase Synthesis of Polyamine Toxin Analogues:  Potent and Selective Antagonists of Ca²⁺-Permeable AMPA Receptors
  作者：Hasse Kromann、Sonata Krikstolaityte、Anne J. Andersen、Kim Andersen、Povl Krogsgaard-Larsen、Jerzy W. Jaroszewski、Jan Egebjerg、Kristian Strømgaard

  DOI：10.1021/jm020314s

  日期：2002.12.1

  The wasp toxin philanthotoxin-433 (PhTX-433) is a nonselective and noncompetitive antagonist of ionotropic receptors, such as ionotropic glutamate receptors and nicotinic acetylcholine receptors. Polyamine toxins are extensively used for the characterization of subtypes of ionotropic glutamate receptors, in particular Ca2+-permeable AMPA and kainate receptors. We have previously shown that an analogue of PhTX-433 with one of the amino groups replaced by a methylene group, philanthotoxin-83 (PhTX-83) is a selective and potent antagonist of AMPA receptors. We now describe the solid-phase synthesis of analogues of PhTX-83 and the electrophysiological characterization of these analogues on cloned AMPA and kainate receptors. The polyamine portion of PhTX-83 was modified systematically by chaniging the position. of the. secondary amino group along the polyamine chain. In another series of analogues, the acyl moiety of PhTX-83 was replaced by acids of different size and lipophilicity. Using electrophysiological techniques, PhTX-56 was shown to be a highly potent (K-i = 3.3 +/- 0.78 nM) and voltage-dependent antagonist of homomeric GluR1 receptors and was more than 1000-fold less potent when tested on heteromeric GluR1+GluR2, as well as homomeric GluR5(Q) receptors, thus being selective for Ca2+-permeable AMPA receptors. Variation of the acyl group of PhTX-83 had only minor effect on antagonist potency at homomeric GluR receptors but led to a significant decrease in the voltage-dependence. In conclusion, PhTX-56 is a novel, very potent, and selective antagonist of Ca2+-permeable AMPA receptors and is a promising tool for structure/function studies of the ion channel of the AMPA receptor.