N-(4-((2,6-diaminopyrimidin-4-yloxy)methyl)benzyl)-2,2,2-trifluoroacetamide | 863772-08-1

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 二嗪类
• 英文名称: N-(4-((2,6-diaminopyrimidin-4-yloxy)methyl)benzyl)-2,2,2-trifluoroacetamide
• 英文别名: 2,6-Diamino-4-[4-(2,2,2-trifluoro-acetamidomethyl)-benzyloxy]-pyrimidine；N-[[4-[(2,6-diaminopyrimidin-4-yl)oxymethyl]phenyl]methyl]-2,2,2-trifluoroacetamide
• CAS: 863772-08-1
• 化学式: C₁₄H₁₄F₃N₅O₂
• 分子量: 341.293
• InChiKey: YUEYAEFZMFLJST-UHFFFAOYSA-N

物化性质

• 密度：
  1.441±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  1.5
• 重原子数：
  24
• 可旋转键数：
  5
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.21
• 拓扑面积：
  116
• 氢给体数：
  3
• 氢受体数：
  9

反应信息

• 作为反应物：
  描述：

  N-(4-((2,6-diaminopyrimidin-4-yloxy)methyl)benzyl)-2,2,2-trifluoroacetamide 在 溶剂黄146 、 盐酸-N-乙基-Nˊ-(3-二甲氨基丙基)碳二亚胺 、 N,N-二异丙基乙胺 、 potassium hydroxide 、 sodium nitrite 作用下， 以 甲醇 、 水 、 丙酮 为溶剂， 反应 4.5h， 生成 2,5-dioxopyrrolidin-1-yl 3-(2-amino-6-((4-((2,2,2-trifluoroacetamido)methyl)benzyl)oxy)-9H-purin-8-yl)propanoate
  参考文献：
  名称：

  Real-Time Measurements of Protein Dynamics Using Fluorescence Activation-Coupled Protein Labeling Method

  摘要：

  We present a fluorescence activation-coupled protein labeling (FAPL) method, which employs small-molecular probes that exhibit almost no basal fluorescence but acquire strong fluorescence upon covalent binding to tag-proteins. This method enables real-time imaging of protein labeling without any washout process and is uniquely suitable for real-time imaging of protein dynamics on the cell surface. We applied this method to address the spatiotemporal dynamics of the EGF receptor during cell migration.

  DOI：

  10.1021/ja200225m
• 作为产物：
  描述：

  4-胺甲基苯甲醇 在 吡啶 、 sodium 、 N,N-二异丙基乙胺 作用下， 以 乙醇 、 对二甲苯 为溶剂， 反应 5.0h， 生成 N-(4-((2,6-diaminopyrimidin-4-yloxy)methyl)benzyl)-2,2,2-trifluoroacetamide
  参考文献：
  名称：

  Real-Time Measurements of Protein Dynamics Using Fluorescence Activation-Coupled Protein Labeling Method

  摘要：

  We present a fluorescence activation-coupled protein labeling (FAPL) method, which employs small-molecular probes that exhibit almost no basal fluorescence but acquire strong fluorescence upon covalent binding to tag-proteins. This method enables real-time imaging of protein labeling without any washout process and is uniquely suitable for real-time imaging of protein dynamics on the cell surface. We applied this method to address the spatiotemporal dynamics of the EGF receptor during cell migration.

  DOI：

  10.1021/ja200225m

文献信息

• Specific Substrates for O6-Alkylguanine-Dna Alkyltransferase
  申请人：Jaccard Hughes

  公开号：US20070243568A1

  公开（公告）日：2007-10-18

  The invention relates to substrates for O 6 -alkylguanine-DNA alkyltransferases (AGT) of formula R 1 -A-X—CH 2 —R 3 —R 4 -L 1 , wherein A is a group recognized by AGT as a substrate, X is oxygen or sulfur, R 1 is a group —R 2 -L 2 or a group R 5 , R 2 and R 4 are, independently of each other, a linker, R 3 is an aromatic or a heteroaromatic group, or an optionally substituted unsaturated alkyl, cycloalkyl or heterocyclyl group with the double bond connected to CH 2 , R 5 is arylmethyl or heteroarylmethyl or an optionally substituted cycloalkyl, cycloalkenyl or heterocyclyl group, L 1 is a label, a plurality of same or different labels, a bond connecting R 4 to A forming a cyclic substrate, or a further group —R 3 CH 2 —X-A-R 1 , and L 2 is a label or a plurality of same or different labels. The invention further relates to methods of transferring a label from these substrates to O 6 -alkylguanine-DNA alkyltransferases (AGT) and AGT fusion proteins.

  本发明涉及O6-烷基鸟嘌呤-DNA烷基转移酶（AGT）的底物，其化学式为R1-A-X—CH2—R3—R4-L1，其中A是被AGT识别为底物的基团，X是氧或硫，R1是一个基团，可以是—R2-L2或R5，R2和R4分别是连接基团，R3是芳香或杂芳基团，或者是一个可选取代的不饱和烷基、环烷基或杂环基团，其双键连接到CH2，R5是芳基甲基或杂芳基甲基或可选取代的环烷基、环烯基或杂环基团，L1是标记，多个相同或不同的标记，或者是连接R4和A形成环状底物的键，或者是进一步的基团—R3CH2—X-A-R1，L2是标记或多个相同或不同的标记。本发明还涉及将这些底物上的标记转移给O6-烷基鸟嘌呤-DNA烷基转移酶（AGT）和AGT融合蛋白的方法。
• Specific substrates for O6-alkylguanine-DNA alkyltransferase
  申请人：Ecole Polytechnique Federale de Lausanne

  公开号：US08163479B2

  公开（公告）日：2012-04-24

  The invention relates to substrates for O6-alkylguanine-DNA alkyltransferases (AGT) of formula R1-A-X—CH2—R3—R4-L1, wherein A is a group recognized by AGT as a substrate, X is oxygen or sulfur, R1 is a group —R2-L2 or a group R5, R2 and R4 are, independently of each other, a linker, R3 is an aromatic or a heteroaromatic group, or an optionally substituted unsaturated alkyl, cycloalkyl or heterocyclyl group with the double bond connected to CH2, R5 is arylmethyl or heteroarylmethyl or an optionally substituted cycloalkyl, cycloalkenyl or heterocyclyl group, L1 is a label, a plurality of same or different labels, a bond connecting R4 to A forming a cyclic substrate, or a further group —R3—CH2—X-A-R1, and L2 is a label or a plurality of same or different labels. The invention further relates to methods of transferring a label from these substrates to O6-alkylguanine-DNA alkyltransferases (AGT) and AGT fusion proteins.

  本发明涉及O6-烷基鸟嘌呤-DNA烷基转移酶（AGT）的底物，其化学式为R1-A-X—CH2—R3—R4-L1，其中A是被AGT识别为底物的基团，X为氧或硫，R1是一个基团—R2-L2或一个基团R5，R2和R4分别是连接器，R3是芳香或杂环芳香基，或者是一个可选取代的不饱和烷基、环烷基或杂环烷基，其双键连接到CH2，R5是芳基甲基或杂芳基甲基或一个可选取代的环烷基、环烯基或杂环烷基，L1是标签，若干个相同或不同的标签，或者是连接R4到A形成一个环形底物的键，或者是进一步的基团—R3—CH2—X-A-R1，L2是一个标签或若干个相同或不同的标签。本发明还涉及将这些底物中的标签转移至O6-烷基鸟嘌呤-DNA烷基转移酶（AGT）和AGT融合蛋白的方法。
• SPECIFIC SUBSTRATES FOR O6-ALKYLGUANINE-DNA ALKYLTRANSFERASE
  申请人：EPFL Ecole Polytechnique Fédérale de Lausanne

  公开号：EP1730298B1

  公开（公告）日：2015-11-11
• US8163479B2
  申请人：——

  公开号：US8163479B2

  公开（公告）日：2012-04-24
• Real-Time Measurements of Protein Dynamics Using Fluorescence Activation-Coupled Protein Labeling Method
  作者：Toru Komatsu、Kai Johnsson、Hiroyuki Okuno、Haruhiko Bito、Takanari Inoue、Tetsuo Nagano、Yasuteru Urano

  DOI：10.1021/ja200225m

  日期：2011.5.4

  We present a fluorescence activation-coupled protein labeling (FAPL) method, which employs small-molecular probes that exhibit almost no basal fluorescence but acquire strong fluorescence upon covalent binding to tag-proteins. This method enables real-time imaging of protein labeling without any washout process and is uniquely suitable for real-time imaging of protein dynamics on the cell surface. We applied this method to address the spatiotemporal dynamics of the EGF receptor during cell migration.