2,2,2-trifluoroethyl 2-(octanamido)acetate | 1100753-75-0

• 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: 2,2,2-trifluoroethyl 2-(octanamido)acetate
• 英文别名: N-octanoylglycine 2,2,2-trifluoroethyl ester；N-octanoylglycine trifluoroethyl ester；n-heptylCONHCH2CO2CH2CF3；2,2,2-Trifluoroethyl 2-(octanoylamino)acetate
• CAS: 1100753-75-0
• 化学式: C₁₂H₂₀F₃NO₃
• 分子量: 283.291
• InChiKey: QBAMGJJTUGKHOB-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.6
• 重原子数：
  19
• 可旋转键数：
  10
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.83
• 拓扑面积：
  55.4
• 氢给体数：
  1
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  2,2,2-trifluoroethyl 2-(octanamido)acetate 、 (+/-)-1-(1-naphthyl)propan-2-amine 在 alkaline protease 作用下， 以 四氢呋喃 、 3-甲基-3-戊醇 为溶剂， 反应 15.0h， 生成 N-(((S)-1-(naphthalen-4-yl)propan-2-ylcarbamoyl)methyl)octanamide
  参考文献：
  名称：

  En Route to (S)-Selective Chemoenzymatic Dynamic Kinetic Resolution of Aliphatic Amines. One-Pot KR/Racemization/KR Sequence Leading to (S)-Amides

  摘要：

  A one-pot sequential process, involving a radical racemization and an enzymatic resolution, provides access to (S)-amides, from racemic amines, with ee and yields ranging from 78 to 94% and 58 to 80%, respectively.

  DOI：

  10.1021/jo900074w
• 作为产物：
  描述：

  2,2,2-三氟乙醇 、 辛酰甘氨酸 在 N,N-二环己脲 作用下， 以 氯仿 为溶剂， 反应 15.0h， 以70%的产率得到2,2,2-trifluoroethyl 2-(octanamido)acetate
  参考文献：
  名称：

  N-酰基甘氨酸盐在丝氨酸蛋白酶催化的胺的动力学拆分中作为酰基供体。提高选择性和反应速率。

  摘要：

  通过使用碱性蛋白酶作为催化剂，N-辛酰基甘氨酸三氟乙基酯作为酰基供体，可以实现脂肪族和苄基胺类的酶动力学拆分，从而生成（S）-酰胺。对映选择性在4至244之间，而反应时间则大大缩短，在15分钟至6小时之间。

  DOI：

  10.1039/b812089g

文献信息

• N-Octanoyldimethylglycine Trifluoroethyl Ester, an Acyl Donor Leading to Highly Enantioselective Protease-Catalysed Kinetic Resolution of Amines
  作者：Severine Queyroy、Nicolas Vanthuyne、Stéphane Gastaldi、Michèle P. Bertrand、Gérard Gil

  DOI：10.1002/adsc.201100993

  日期：2012.6.18

  The use of N‐octanoyldimethylglycine trifluoroethyl ester as acyl donor in the kinetic resolution of aliphatic amines catalysed by proteases led to enantiomeric ratios >200 in most cases. The resolutions mediated by Protex 6L were shown to be much faster than the resolutions achieved with the most efficient commercially available serine proteases, i.e., alkaline protease, Properase 1600L, and Subtilisin

  在大多数情况下，在蛋白酶催化的脂肪族胺的动力学拆分中，使用N-辛酰基二甲基甘氨酸三氟乙基酯作为酰基供体会导致对映体比率> 200。已证明，由Protex 6L介导的分辨率比使用最有效的市售丝氨酸蛋白酶（即碱性蛋白酶，Properase 1600L和枯草杆菌蛋白酶）获得的分辨率快得多。
• Proteases screening for the kinetic resolution of amines with N-acyl α-amino acid trifluoromethyl esters: automated docking approach of binding energies using Subtilisin Novo as a prototype for serine proteases
  作者：Anne-Lise Bottalla、Séverine Queyroy、Nadia Azzi-Schue、Nicolas Vanthuyne、Stéphane Gastaldi、Michèle P. Bertrand、Gérard Gil

  DOI：10.1016/j.tetasy.2009.11.013

  日期：2009.12

  The screening of a panel of 17 proteases resulted in the selection of 4 serine proteases for the resolution of 3-amino-1-phenylbutane. The latter were used to determine the best acyl donor from a series of N-acyl alpha-amino acid trifluoroethyl esters selected as peptide mimetics (E factor up to 99). The results were correlated to an automated docking determination of their binding affinities for Subtilisin Novo. (C) 2009 Elsevier Ltd. All rights reserved.
• N-Acyl glycinates as acyl donors in serine protease-catalyzed kinetic resolution of amines. Improvement of selectivity and reaction rate
  作者：Malek Nechab、Lahssen El Blidi、Nicolas Vanthuyne、Stéphane Gastaldi、Michèle P. Bertrand、Gérard Gil

  DOI：10.1039/b812089g

  日期：——

  Enzymatic kinetic resolution of aliphatic and benzylic amines leading to (S)-amides was achieved by using alkaline protease as the catalyst and N-octanoyl glycine trifluoroethyl ester as the acyl donor; enantioselectivity ranged between 4 to 244, while reaction times were dramatically shortened and ranged between 15 min to 6 h.

  通过使用碱性蛋白酶作为催化剂，N-辛酰基甘氨酸三氟乙基酯作为酰基供体，可以实现脂肪族和苄基胺类的酶动力学拆分，从而生成（S）-酰胺。对映选择性在4至244之间，而反应时间则大大缩短，在15分钟至6小时之间。
• En Route to (<i>S</i>)-Selective Chemoenzymatic Dynamic Kinetic Resolution of Aliphatic Amines. One-Pot KR/Racemization/KR Sequence Leading to (<i>S</i>)-Amides
  作者：Lahssen El Blidi、Malek Nechab、Nicolas Vanthuyne、Stéphane Gastaldi、Michèle P. Bertrand、Gérard Gil

  DOI：10.1021/jo900074w

  日期：2009.4.3

  A one-pot sequential process, involving a radical racemization and an enzymatic resolution, provides access to (S)-amides, from racemic amines, with ee and yields ranging from 78 to 94% and 58 to 80%, respectively.