di-tert-butyl ((2S,2'S)-((3-oxo-3H-spiro[isobenzofuran-1,9'-xanthene]-3',6'-diyl)bis(azanediyl))bis(1-oxo-3-phenylpropane-1,2-diyl))dicarbamate | 1001200-94-7

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 苯并吡喃
• 英文名称: di-tert-butyl ((2S,2'S)-((3-oxo-3H-spiro[isobenzofuran-1,9'-xanthene]-3',6'-diyl)bis(azanediyl))bis(1-oxo-3-phenylpropane-1,2-diyl))dicarbamate
• CAS: 1001200-94-7
• 化学式: C₄₈H₄₈N₄O₉
• 分子量: 824.931
• InChiKey: PMCJXXPRYQSYPS-UWXQCODUSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  8.4
• 重原子数：
  61.0
• 可旋转键数：
  10.0
• 环数：
  7.0
• sp3杂化的碳原子比例：
  0.27
• 拓扑面积：
  170.39
• 氢给体数：
  4.0
• 氢受体数：
  9.0

反应信息

• 作为反应物：
  描述：

  di-tert-butyl ((2S,2'S)-((3-oxo-3H-spiro[isobenzofuran-1,9'-xanthene]-3',6'-diyl)bis(azanediyl))bis(1-oxo-3-phenylpropane-1,2-diyl))dicarbamate 在 三氟乙酸 作用下， 以 二氯甲烷 为溶剂， 反应 1.0h， 生成 (2S,2'S)-N,N'-(3-oxo-3H-spiro[isobenzofuran-1,9'-xanthene]-3',6'-diyl)bis(2-amino-3-phenylpropanamide)
  参考文献：
  名称：

  Dynamic Disorder and Stepwise Deactivation in a Chymotrypsin Catalyzed Hydrolysis Reaction

  摘要：

  In situ observation of the catalytic activity of individual M-chymotrypsin enzymes reveals a novel pathway for spontaneous deactivation. Rather than deactivating abruptly in a one-step process, the enzyme seems to struggle for life; the activity decreases stepwise with intermittent inactive periods before deactivating irreversibly. During the active periods, dynamic disorder and memory effects are observed, originating from conformational fluctuations within the enzyme's structure.

  DOI：

  10.1021/ja077621d
• 作为产物：
  描述：

  BOC-L-苯丙氨酸 、 rhodamine 110 在 4-二甲氨基吡啶 、 N,N'-二异丙基碳二亚胺 作用下， 以 二氯甲烷 为溶剂， 反应 20.0h， 以53%的产率得到di-tert-butyl ((2S,2'S)-((3-oxo-3H-spiro[isobenzofuran-1,9'-xanthene]-3',6'-diyl)bis(azanediyl))bis(1-oxo-3-phenylpropane-1,2-diyl))dicarbamate
  参考文献：
  名称：

  Dynamic Disorder and Stepwise Deactivation in a Chymotrypsin Catalyzed Hydrolysis Reaction

  摘要：

  In situ observation of the catalytic activity of individual M-chymotrypsin enzymes reveals a novel pathway for spontaneous deactivation. Rather than deactivating abruptly in a one-step process, the enzyme seems to struggle for life; the activity decreases stepwise with intermittent inactive periods before deactivating irreversibly. During the active periods, dynamic disorder and memory effects are observed, originating from conformational fluctuations within the enzyme's structure.

  DOI：

  10.1021/ja077621d

文献信息

• Morpholinecarbonyl-Rhodamine 110 Based Substrates for the Determination of Protease Activity with Accurate Kinetic Parameters
  作者：Tatyana G. Terentyeva、Wim Van Rossom、Mark Van der Auweraer、Kerstin Blank、Johan Hofkens

  DOI：10.1021/bc2001038

  日期：2011.10.19

  Commonly used fluorogenic substrate analogues for the detection of protease activity contain two enzyme-cleavable bonds conjugated to the fluorophore. Enzymatic cleavage follows a two-step reaction with a monoamide intermediate. This intermediate shows fluorescence at the same wavelength as the final product complicating the kinetic analysis of fluorescence-based assays. Fluorogenic substrate analogues for a-chymotrypsin with one cleavable peptide bond have been prepared from morpholinecarbonyl-Rhodamine 110 (MC-Rh 110). A comparison of their kinetic properties with the corresponding (peptide)(2)-Rh110 derivatives revealed that these frequently used double-substituted substrate analogues yield only apparent Km and km, values that are quite different from the kinetic parameters obtained from the monosubstituted MC-Rh110 based substrate analogues. Although both the monoamide intermediate and MC-Rh110 are monosubstituted Rhodarnine 110 derivatives, they show different spectroscopic properties. The data from the spectroscopic analysis clearly show that these properties are directly related to the electron structure of the fluorophore and not to the previously proposed equilibrium between the lactone form and the open ionic form of the fluorophore. This knowledge about the determinants of the spectroscopic properties of monosubstituted Rhodamine 110 introduces a way for a more systematic development of new fluorogenic protease substrate analogues.