2-[2-[2-(biotinylaminoethoxy)ethoxy]ethoxy]-4-[3-(trifluoromethyl)-3H-diazirin-3-yl]benzyloxyamine | 308085-26-9

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 生物素及其衍生物
• 英文名称: 2-[2-[2-(biotinylaminoethoxy)ethoxy]ethoxy]-4-[3-(trifluoromethyl)-3H-diazirin-3-yl]benzyloxyamine
• 英文别名: (3aS,4S,6aR)-N-[2-[2-[2-[2-[(Aminooxy)methyl]-5-[3-(trifluoromethyl)-3H-diazirin-3-yl]phenoxy]ethoxy]ethoxy]ethyl]hexahydro-2-oxo-1H-thieno[3,4-d]imidazole-4-pentanamide；5-[(3aS,4S,6aR)-2-oxo-1,3,3a,4,6,6a-hexahydrothieno[3,4-d]imidazol-4-yl]-N-[2-[2-[2-[2-(aminooxymethyl)-5-[3-(trifluoromethyl)diazirin-3-yl]phenoxy]ethoxy]ethoxy]ethyl]pentanamide
• CAS: 308085-26-9
• 化学式: C₂₅H₃₅F₃N₆O₆S
• 分子量: 604.651
• InChiKey: XSAUCFKOSLUKNT-VCOUNFBDSA-N

物化性质

• 密度：
  1.53±0.1 g/cm3 (20 ºC 760 Torr)

计算性质

• 辛醇/水分配系数(LogP)：
  1.4
• 重原子数：
  41
• 可旋转键数：
  18
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.68
• 拓扑面积：
  183
• 氢给体数：
  4
• 氢受体数：
  13

反应信息

• 作为反应物：
  描述：

  二碳酸二叔丁酯 、 2-[2-[2-(biotinylaminoethoxy)ethoxy]ethoxy]-4-[3-(trifluoromethyl)-3H-diazirin-3-yl]benzyloxyamine 在 三乙胺 作用下， 以 氯仿 、 乙腈 为溶剂， 反应 14.0h， 以95%的产率得到Affilight-CHO
  参考文献：
  名称：

  Phenyldiazirine compounds and photoaffinity labeling reagent

  摘要：

  这项发明提供了一种光反应性标记试剂，包括一种新型生物素化苯基重氮化合物；一种光亲和标记试剂，包括一种糖链连接的生物素化苯基重氮化合物，其中将糖类化合物引入到该新型化合物中；以及用于该试剂的一种新型重氮化合物。该发明涵盖以下化学式（II）的生物素化苯基重氮化合物；一种用于合成上述化合物的中间体苯基重氮化合物；从化学式（II）的化合物和糖类化合物衍生的糖链连接的生物素化苯基重氮化合物及其制造方法；包含化学式（II）的化合物的光反应性标记试剂；包含糖链连接的生物素化苯基重氮化合物的光亲和标记试剂；以及使用该试剂标记糖类受体的方法。

  公开号：

  US06903223B1
• 作为产物：
  描述：

  Affilight-CHO 在 三氟乙酸 作用下， 以 二氯甲烷 为溶剂， 反应 1.0h， 生成 2-[2-[2-(biotinylaminoethoxy)ethoxy]ethoxy]-4-[3-(trifluoromethyl)-3H-diazirin-3-yl]benzyloxyamine
  参考文献：
  名称：

  Photoaffinity Labeling of Sialidase with a Biotin-Conjugated Phenylaminodiazirine Derivative of 2,3-Didehydro-2-deoxy-N-acetylneuraminic Acid

  摘要：

  合成了一种 2,3-二脱氢-2-脱氧-N-乙酰神经氨酸（DANA）的生物素共轭可光激活的苯氨基二氮氨酸衍生物，用于识别硅氨酸酶。光标记化合物保留了硅氨酸的游离羧基和 N-乙酰取代基，这两个基团对硅氨酸酶的识别和酶活性非常重要，这一点已通过分析方法得到证实。合成的化合物和 DANA 能竞争性地抑制海星的硅糖苷酶，其 Ki 值分别为 7.6 μM和 4.6 μM。标记化合物与硅糖苷酶的光结合随辐照时间的延长而增加；超过 10 分钟的辐照可使光结合率达到 90%，加入竞争性抑制剂可完全抑制标记。用高效凝胶过滤色谱法纯化的海星硅糖苷酶进行了光亲和标记。光标记化合物揭示出一条 50 kDa 的条带含有硅糖苷酶的活性位点，在竞争性抑制剂存在的情况下，标记完全受阻。在反应混合物中加入热失活的标准蛋白糜蛋白酶原 A 可确保标记的特异性。

  DOI：

  10.1248/bpb.31.352

文献信息

• Detection of 210 kDa receptor protein for a leaf-movement factor by using novel photoaffinity probes
  作者：Tomohiko Fujii、Yoshiyuki Manabe、Takanori Sugimoto、Minoru Ueda

  DOI：10.1016/j.tet.2005.06.022

  日期：2005.8

  Circadian rhythmic plant leaf-movement, called nyctinasty, is controlled by a time-course change in the internal concentration of the leaf-movement factor in the plant body. We revealed that specific binding proteins (210 and 180 kDa) for the leaf-movement factor, potassium lespedezate (1), are contained in the plasma membrane of the plant motor cell by using novel synthetic photoaffinity probes. These proteins are localized on the motor cell in the plant body, and would be potential receptors for the leaf-movement factor to control the leaf-movement. Our study is a rare successful result of the detection of membrane receptors by using a synthetic photoaffinity probe designed on a biologically active natural product. And these results also advance a guideline for probe design towards successful photoaffinity labeling. (c) 2005 Elsevier Ltd. All rights reserved.
• One-Step Synthesis of Biotinyl Photoprobes from Unprotected Carbohydrates
  作者：Yasumaru Hatanaka、Uwe Kempin、Park Jong-Jip

  DOI：10.1021/jo000414a

  日期：2000.9.1

  A simple and versatile approach for the preparation of carbohydrate photoprobes has been developed. By a single-step reaction at 37 degrees C, a biotinylated carbene-generating unit was introduced to the reducing end of unprotected carbohydrates. Micromole quantities of N-acetyllactosamine, Lewis X trisaccharide, and sialyl Lewis X tetrasaccharide were easily converted to their biotinylated photoreactive analogues, which enabled the nonradioisotopic chemiluminescent detection of the photolabeled products. Thus, a sequence of lectin photoaffinity labeling, from the probe synthesis to the detection of labeled protein, was readily accomplished within one week. Our strategy may be applicable to any aldehyde-bearing ligand.
• The effect of structural differences in the reducing terminus of sugars on the binding affinity of carbohydrates and proteins analyzed using photoaffinity labeling
  作者：Isao Ohtsuka、Yutaka Sadakane、Mari Higuchi、Noriyasu Hada、Junko Hada、Nobuko Kakiuchi、Akiyo Sakushima

  DOI：10.1016/j.bmc.2010.11.067

  日期：2011.1

  Because carbohydrates and proteins bind with such low affinity, the nature of their interactions is not clear. Photoaffinity labeling with diazirin groups is useful for elucidating the roles of carbohydrates in these binding processes. However, when carbohydrate probes are synthesized according to this conventional method, the reducing terminus of the sugar is opened to provide an acyclic structure. Because greater elucidation of carbohydrate-protein interactions requires a closed-ring carbohydrate in addition to the photoreactive group, we synthesized new molecular tools. The carbohydrate ligands were synthesized in three steps (glycosylation with allyl alcohol, deprotection, and ozonolysis). Specific binding proteins for carbohydrate ligands were obtained by photoaffinity labeling. Closed ring-type carbohydrate ligands, in which the reducing sugar is closed, bound to lectins more strongly than open ring-type sugars. Carbohydrate to protein binding was observed using AFM. (C) 2010 Elsevier Ltd. All rights reserved.
• The development of new molecular tools containing a chemically synthesized carbohydrate ligand for the elucidation of carbohydrate roles via photoaffinity labeling: Carbohydrate–protein interactions are affected by the structures of the glycosidic bonds and the reducing-end sugar
  作者：Isao Ohtsuka、Yutaka Sadakane、Noriyasu Hada、Mari Higuchi、Toshiyuki Atsumi、Nobuko Kakiuchi

  DOI：10.1016/j.bmc.2014.06.049

  日期：2014.8

  Photoaffinity labeling technology is a highly efficient method for cloning carbohydrate-binding proteins. When the carbohydrate probes are synthesized according to conventional methods, however, the reducing terminus of the sugar is opened to provide an acyclic structure. Our continued efforts to solve this problem led to the development of new molecular tools with an oligosaccharide structure that contains a phenyldiazirine group for the elucidation of carbohydrate-protein interactions. We investigated whether carbohydrate-lectin interactions are affected by differences in the glycosidic formation and synthesized three types of molecular tools containing Galp-GlcpNAc disaccharide ligands and a photoreactive group (1, 2, 3). Photoaffinity labeling validated the recognition of the new ligand by different glycosidic bonds. Photoaffinity labeling also demonstrated that both the reducing end sugar and non-reducing end sugar recognized the Erythrina cristagalli agglutinin.