(2-aminomethyl)(6-azidomethyl)pyridine | 628308-54-3

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 吡啶及其衍生物
• 英文名称: (2-aminomethyl)(6-azidomethyl)pyridine
• 英文别名: [6-(Azidomethyl)pyridin-2-yl]methanamine
• CAS: 628308-54-3
• 化学式: C₇H₉N₅
• 分子量: 163.182
• InChiKey: WXUFUUCSGLQUKV-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.7
• 重原子数：
  12
• 可旋转键数：
  3
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.29
• 拓扑面积：
  53.3
• 氢给体数：
  1
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  (2-aminomethyl)(6-azidomethyl)pyridine 在 镍 氢气 、 三乙酰氧基硼氢化钠 作用下， 生成 (2-{[6-(tert-Butoxycarbonylamino-methyl)-pyridin-2-ylmethyl]-amino}-ethyl)-carbamic acid benzyl ester
  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-吡啶二甲醇 在 氯化亚砜 、 sodium azide 、 sodium carbonate 、 肼 作用下， 生成 (2-aminomethyl)(6-azidomethyl)pyridine
  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

• 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.