4-(((2S)-1-(((2S)-1-((2S)-2-(((2S)-1-((3'-(morpholine-4-carboxamido)-3-oxo-3H-spiro[isobenzofuran-1,9'-xanthen]-6'-yl)amino)-1-oxo-3-phenylpropan-2-yl)carbamoyl)pyrrolidin-1-yl)-1-oxopropan-2-yl)amino)-1-oxopropan-2-yl)amino)-4-oxobutanoic acid | 1336878-70-6

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: 4-(((2S)-1-(((2S)-1-((2S)-2-(((2S)-1-((3'-(morpholine-4-carboxamido)-3-oxo-3H-spiro[isobenzofuran-1,9'-xanthen]-6'-yl)amino)-1-oxo-3-phenylpropan-2-yl)carbamoyl)pyrrolidin-1-yl)-1-oxopropan-2-yl)amino)-1-oxopropan-2-yl)amino)-4-oxobutanoic acid
• CAS: 1336878-70-6
• 化学式: C₄₉H₅₁N₇O₁₂
• 分子量: 929.984
• InChiKey: XSGALJFXBBZNMI-HMTALLNJSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.65
• 重原子数：
  68.0
• 可旋转键数：
  14.0
• 环数：
  8.0
• sp3杂化的碳原子比例：
  0.35
• 拓扑面积：
  251.11
• 氢给体数：
  6.0
• 氢受体数：
  11.0

反应信息

• 作为反应物：
  描述：

  4-(((2S)-1-(((2S)-1-((2S)-2-(((2S)-1-((3'-(morpholine-4-carboxamido)-3-oxo-3H-spiro[isobenzofuran-1,9'-xanthen]-6'-yl)amino)-1-oxo-3-phenylpropan-2-yl)carbamoyl)pyrrolidin-1-yl)-1-oxopropan-2-yl)amino)-1-oxopropan-2-yl)amino)-4-oxobutanoic acid 在 α-chymotrypsin from bovine pancreas 作用下， 以 二甲基亚砜 为溶剂， 生成 2-(3-iminio-6-(morpholine-4-carboxamido)-3H-xanthen-9-yl)benzoate
  参考文献：
  名称：

  Morpholinecarbonyl-Rhodamine 110 Based Substrates for the Determination of Protease Activity with Accurate Kinetic Parameters

  摘要：

  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.

  DOI：

  10.1021/bc2001038
• 作为产物：
  描述：

  在 α-chymotrypsin from bovine pancreas 、 O-(benzotriazol-1-yl)-N,N,N',N'-tetramethyluronium tetrafluoroborate 、 N,N-二异丙基乙胺 、 三氟乙酸 作用下， 以 二氯甲烷 、 二甲基亚砜 、 N,N-二甲基甲酰胺 为溶剂， 反应 45.0h， 生成 4-(((2S)-1-(((2S)-1-((2S)-2-(((2S)-1-((3'-(morpholine-4-carboxamido)-3-oxo-3H-spiro[isobenzofuran-1,9'-xanthen]-6'-yl)amino)-1-oxo-3-phenylpropan-2-yl)carbamoyl)pyrrolidin-1-yl)-1-oxopropan-2-yl)amino)-1-oxopropan-2-yl)amino)-4-oxobutanoic acid
  参考文献：
  名称：

  Morpholinecarbonyl-Rhodamine 110 Based Substrates for the Determination of Protease Activity with Accurate Kinetic Parameters

  摘要：

  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.

  DOI：

  10.1021/bc2001038