10-{[({tert-Butoxycarbonylmethyl-[2-(9H-fluoren-9-ylmethoxycarbonylamino)-ethyl]-carbamoyl}-methyl)-carbamoyl]-methyl}-1,4,7,10-tetraaza-cyclododecane-1,4,7-tricarboxylic acid tribenzyl ester | 473894-90-5

• 分子结构分类: 有机化合物 - 苯类化合物 - 芴
• 英文名称: 10-{[({tert-Butoxycarbonylmethyl-[2-(9H-fluoren-9-ylmethoxycarbonylamino)-ethyl]-carbamoyl}-methyl)-carbamoyl]-methyl}-1,4,7,10-tetraaza-cyclododecane-1,4,7-tricarboxylic acid tribenzyl ester
• CAS: 473894-90-5
• 化学式: C₅₉H₆₉N₇O₁₂
• 分子量: 1068.24
• InChiKey: AOMQDDWLJPZEMO-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  7.04
• 重原子数：
  78.0
• 可旋转键数：
  17.0
• 环数：
  7.0
• sp3杂化的碳原子比例：
  0.37
• 拓扑面积：
  205.9
• 氢给体数：
  2.0
• 氢受体数：
  13.0

反应信息

• 作为反应物：
  描述：

  10-{[({tert-Butoxycarbonylmethyl-[2-(9H-fluoren-9-ylmethoxycarbonylamino)-ethyl]-carbamoyl}-methyl)-carbamoyl]-methyl}-1,4,7,10-tetraaza-cyclododecane-1,4,7-tricarboxylic acid tribenzyl ester 在 sodium hydroxide 作用下， 生成 10-{[({Carboxymethyl-[2-(9H-fluoren-9-ylmethoxycarbonylamino)-ethyl]-carbamoyl}-methyl)-carbamoyl]-methyl}-1,4,7,10-tetraaza-cyclododecane-1,4,7-tricarboxylic acid tribenzyl 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：

  1,4,7-tris-(benzyloxycarbonyl)-10-(ethoxycarbonylmethyl)-1,4,7,10-tetraazacyclododecane 在 sodium hydroxide 、 O-(1H-benzotriazol-1-yl)-N,N,N',N'-tetramethyluronium hexafluorophosphate 作用下， 生成 10-{[({tert-Butoxycarbonylmethyl-[2-(9H-fluoren-9-ylmethoxycarbonylamino)-ethyl]-carbamoyl}-methyl)-carbamoyl]-methyl}-1,4,7,10-tetraaza-cyclododecane-1,4,7-tricarboxylic acid tribenzyl 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