THPTA(OAc)3 | 1208358-31-9

• 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: THPTA(OAc)3
• 英文别名: tris(3-acetoxypropyltriazolylmethyl)amine
• CAS: 1208358-31-9
• 化学式: C₂₄H₃₆N₁₀O₆
• 分子量: 560.613
• InChiKey: DLAMPKLASVVHKE-UHFFFAOYSA-N

物化性质

• 沸点：
  727.5±70.0 °C(Predicted)
• 密度：
  1.35±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  0.52
• 重原子数：
  40.0
• 可旋转键数：
  18.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.62
• 拓扑面积：
  174.27
• 氢给体数：
  0.0
• 氢受体数：
  16.0

反应信息

• 作为反应物：
  描述：

  THPTA(OAc)3 在 甲醇 、 氨 作用下， 以 二氯甲烷 为溶剂， 以86%的产率得到三(3-羟丙基三唑甲基)胺
  参考文献：
  名称：

  超分子树状大分子：通过程序自组装和可调节的热响应性方便地合成

  摘要：

  我们在这里报告了热敏树枝状聚合物的非共价合成。短寡核苷酸链通过“点击化学”与树突的焦点相连，在存在金属离子的情况下，利用四链体形成来驱动自组装过程。可以利用这些非共价装配体的动态性质来创建树枝状聚合物的组合文库，这是由两个组分的共同装配所证明的。这些超分子树状聚合物显示出可通过改变寡核苷酸链中的模板阳离子或鸟嘌呤数量来调节的热响应行为。

  DOI：

  10.1002/chem.201103051
• 作为产物：
  描述：

  丁基氨基甲酸酯 在 sodium azide 、 copper (I) acetate 作用下， 以 四氢呋喃 、 水 为溶剂， 生成 THPTA(OAc)3
  参考文献：
  名称：

  Methods of modifying N-termini of a peptide or protein using transferases

  摘要：

  该发明涉及使用氨酰基tRNA转移酶选择性地修改蛋白质的N-末端的方法。在某些实施例中，该方法包括将蛋白质或肽溶液与转移酶和分子衍生物接触，从而使蛋白质或肽的N-末端与该分子衍生物发生衍生化反应。

  公开号：

  US09376700B2

文献信息

• Controlling the Kinetics of Self-Reproducing Micelles by Catalyst Compartmentalization in a Biphasic System
  作者：Elias A. J. Post、Stephen P. Fletcher

  DOI：10.1021/acs.joc.8b03149

  日期：2019.3.1

  Compartmentalization of reactions is ubiquitous in biochemistry. Self-reproducing lipids are widely studied as chemical models of compartmentalized biological systems. Here, we explore the effect of catalyst location on copper-catalyzed azide-alkyne cycloadditions which drive the self-reproduction of micelles from phase-separated components. Tuning the hydrophilicity of the copper-ligand complex, so that hydro-phobic or -philic catalysts are used in combination with hydro-philic and -phobic coupling partners, provides a wide range of reactivity patterns. Analysis of the kinetic data shows that reactions with a hydrophobic catalyst are faster than with a hydrophilic catalyst. Diffusion-ordered spectroscopy experiments suggest compartmentalization of the hydrophobic catalyst inside micelles while the hydrophilic catalyst remains in the bulk aqueous phase. The autocatalytic effects observed can be tuned by varying reactant structure and coupling a hydrophilic alkyne and hydrophobic azide results in a more pronounced autocatalytic effect. We propose and test a model that rationalizes the observations in terms of the phase behavior of the reaction components and catalysts.
• N-Terminal Protein Modification Using Simple Aminoacyl Transferase Substrates
  作者：Anne M. Wagner、Mark W. Fegley、John B. Warner、Christina L. J. Grindley、Nicholas P. Marotta、E. James Petersson

  DOI：10.1021/ja2055098

  日期：2011.9.28

  Methods for synthetically manipulating protein structure enable greater flexibility in the study of protein function. Previous characterization of the Escherichia coli aminoacyl tRNA transferase (AaT) has shown that it can modify the N-terminus of a protein with an amino acid from a tRNA or a synthetic oligonucleotide donor. Here, we demonstrate that AaT can efficiently use a minimal adenosine substrate, which can be synthesized in one to two steps from readily available starting materials. We have characterized the enzymatic activity of AaT with aminoacyl adenosyl donors and found that reaction products do not inhibit AaT. The use of adenosyl donors removes the substrate limitations imposed by the use of synthetases for tRNA charging and avoids the complex synthesis of an oligonucleotide donor. Thus, our AaT donors increase the potential substrate scope and reaction scale for N-terminal protein modification under conditions that maintain folding.