N-[(6-azidomethyl-2-pyridyl)methyl]phthalimide | 628308-53-2

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 异吲哚及其衍生物
• 英文名称: N-[(6-azidomethyl-2-pyridyl)methyl]phthalimide
• 英文别名: 2-{[6-(Azidomethyl)pyridin-2-yl]methyl}-1H-isoindole-1,3(2H)-dione；2-[[6-(azidomethyl)pyridin-2-yl]methyl]isoindole-1,3-dione
• CAS: 628308-53-2
• 化学式: C₁₅H₁₁N₅O₂
• 分子量: 293.285
• InChiKey: NUOVHULVNYGWBH-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.3
• 重原子数：
  22
• 可旋转键数：
  4
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.13
• 拓扑面积：
  64.6
• 氢给体数：
  0
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  N-[(6-azidomethyl-2-pyridyl)methyl]phthalimide 在 镍 氢气 、 肼 作用下， 生成 1,1-Dimethylethyl N-[[6-(aminomethyl)-2-pyridinyl]methyl]carbamate
  参考文献：
  名称：

  Toward Protein-Cleaving Catalytic Drugs: Artificial Protease Selective for Myoglobin

  摘要：

  A protein-cleaving catalyst highly selective for a disease-related protein can be used as a catalytic drug. As the first protein-cleaving catalyst selective for a protein substrate, a catalyst for myoglobin (Mb) was designed by attaching the Cu(II) or Co(III) complex of cyclen to a binding site searched by a combinatorial method using peptide nucleic acid monomers as building units. Various linkers were inserted between the catalytic Co(III) center and the binding site of the Mb-cleaving catalyst. Kinetic data revealed catalytic turnover of the Mb cleavage by the Cu(II) or Co(III) complex. MALDI-TOF MS revealed cleavage of the polypeptide backbone of Mb at selected positions. N-Terminal sequencing of the cleavage products identified the cleavage site and provided evidence for the hydrolytic nature of the Mb cleavage. Various chelating ligands were tested as the ligand for the Co(III) center of the Mb-cleaving catalyst. Among the nine chelating ligands examined, only cyclen and its triaza-monooxo analogue manifested catalytic activity. (C) 2003 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0968-0896(03)00216-5
• 作为产物：
  描述：

  2,6-二氯甲基吡啶 在 sodium azide 、 sodium carbonate 作用下， 生成 N-[(6-azidomethyl-2-pyridyl)methyl]phthalimide
  参考文献：
  名称：

  Toward Protein-Cleaving Catalytic Drugs: Artificial Protease Selective for Myoglobin

  摘要：

  A protein-cleaving catalyst highly selective for a disease-related protein can be used as a catalytic drug. As the first protein-cleaving catalyst selective for a protein substrate, a catalyst for myoglobin (Mb) was designed by attaching the Cu(II) or Co(III) complex of cyclen to a binding site searched by a combinatorial method using peptide nucleic acid monomers as building units. Various linkers were inserted between the catalytic Co(III) center and the binding site of the Mb-cleaving catalyst. Kinetic data revealed catalytic turnover of the Mb cleavage by the Cu(II) or Co(III) complex. MALDI-TOF MS revealed cleavage of the polypeptide backbone of Mb at selected positions. N-Terminal sequencing of the cleavage products identified the cleavage site and provided evidence for the hydrolytic nature of the Mb cleavage. Various chelating ligands were tested as the ligand for the Co(III) center of the Mb-cleaving catalyst. Among the nine chelating ligands examined, only cyclen and its triaza-monooxo analogue manifested catalytic activity. (C) 2003 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0968-0896(03)00216-5

文献信息

• [EN] AZOLOPYRIMIDINE FOR THE TREATMENT OF CANCER-RELATED DISORDERS<br/>[FR] AZOLOPYRIMIDINE POUR LE TRAITEMENT DE TROUBLES LIÉS AU CANCER
  申请人：ARCUS BIOSCIENCES INC

  公开号：WO2018136700A1

  公开（公告）日：2018-07-26

  Compound that is an inhibitor of at least one of the A2A and A2B adenosine receptors, and compositions containing the compound and methods for synthesizing the compound, are described herein. The use of such compound and compositions for the treatment of a diverse array of diseases, disorders, and conditions, including cancer- and immune-related disorders that are mediated, at least in part, by the adenosine A2A receptor and/or the adenosine A2B receptor.

  本文描述了一种至少抑制A2A和A2B腺苷受体中至少一种的化合物，以及含有该化合物的组合物和合成该化合物的方法。利用这种化合物和组合物治疗各种疾病、紊乱和病况，包括至少部分由腺苷A2A受体和/或腺苷A2B受体介导的癌症和免疫相关紊乱。
• Fluorescence Imaging of Intracellular Cadmium Using a Dual-Excitation Ratiometric Chemosensor
  作者：Masayasu Taki、Mika Desaki、Akio Ojida、Shohei Iyoshi、Tasuku Hirayama、Itaru Hamachi、Yukio Yamamoto

  DOI：10.1021/ja803429z

  日期：2008.9.24

  We described here a coumarin-based dual-excitation ratiometric probe for cadmium, CadMQ. This fluorescence sensor has high quantum yields of 0.59 and 0.70 in the metal-free and Cd2+ bound forms, respectively, and has a dissociation constant of 0.16 nM for Cd2+. CadMQ is cell permeable and locates within the acidic compartments of the cells. We further show that CadMQ is a useful tool to ratiometrically probe the change in the intracellular Cd2+ levels with the use of two excited wavelengths.
• Toward Protein-Cleaving Catalytic Drugs: Artificial Protease Selective for Myoglobin
  作者：Joong Won Jeon、Sang Jun Son、Chang Eun Yoo、In Seok Hong、Junghun Suh

  DOI：10.1016/s0968-0896(03)00216-5

  日期：2003.7

  A protein-cleaving catalyst highly selective for a disease-related protein can be used as a catalytic drug. As the first protein-cleaving catalyst selective for a protein substrate, a catalyst for myoglobin (Mb) was designed by attaching the Cu(II) or Co(III) complex of cyclen to a binding site searched by a combinatorial method using peptide nucleic acid monomers as building units. Various linkers were inserted between the catalytic Co(III) center and the binding site of the Mb-cleaving catalyst. Kinetic data revealed catalytic turnover of the Mb cleavage by the Cu(II) or Co(III) complex. MALDI-TOF MS revealed cleavage of the polypeptide backbone of Mb at selected positions. N-Terminal sequencing of the cleavage products identified the cleavage site and provided evidence for the hydrolytic nature of the Mb cleavage. Various chelating ligands were tested as the ligand for the Co(III) center of the Mb-cleaving catalyst. Among the nine chelating ligands examined, only cyclen and its triaza-monooxo analogue manifested catalytic activity. (C) 2003 Elsevier Science Ltd. All rights reserved.