5-(4-Sulfamoyl-benzylcarbamoyl)-pentanoic acid | 142319-48-0

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: 5-(4-Sulfamoyl-benzylcarbamoyl)-pentanoic acid
• 英文别名: Hexanoic acid, 6-[[[4-(aminosulfonyl)phenyl]methyl]amino]-6-oxo-；6-oxo-6-[(4-sulfamoylphenyl)methylamino]hexanoic acid
• CAS: 142319-48-0
• 化学式: C₁₃H₁₈N₂O₅S
• 分子量: 314.362
• InChiKey: KYFAPMAXEFICOA-UHFFFAOYSA-N

物化性质

• 密度：
  1.341±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -0.3
• 重原子数：
  21
• 可旋转键数：
  8
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.38
• 拓扑面积：
  135
• 氢给体数：
  3
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  5-(4-Sulfamoyl-benzylcarbamoyl)-pentanoic acid 在 1-羟基苯并三唑 、 N,N'-二环己基碳二亚胺 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 2.5h， 生成 4-<3-<<6-<<<4-(aminosulfonyl)phenyl>methyl>amino>-1,6-dioxohexyl>amino>propyl>-4-methylmorpholinium iodide
  参考文献：
  名称：

  通过亲和毛细管电泳确定配体与蛋白质的结合常数：补偿电渗流量。

  摘要：

  本文描述了在迁移时间受电渗变化影响的条件下，亲和毛细管电泳（ACE）对碳酸酐酶B（CAB，EC 4.2.1.1，来自牛红细胞）和带电荷的苯磺酰胺之间的结合常数（Kb）的估计。流动和通过非特异性相互作用伴随配体浓度的变化。目的蛋白和“非相互作用”标记蛋白与中性内标物的迁移时间值的比较为校正可变的电渗流提供了基础。即使存在电渗流量的巨大变化，这些修正也可以估算Kb及其不确定性。

  DOI：

  10.1021/ac00083a003
• 作为产物：
  描述：

  mafenide hydrochloride 在 sodium hydroxide 、 三乙胺 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 14.0h， 生成 5-(4-Sulfamoyl-benzylcarbamoyl)-pentanoic acid
  参考文献：
  名称：

  使用亲和毛细管电泳确定芳基磺酰胺与牛碳酸酐酶结合的动力学和平衡常数。

  摘要：

  亲和毛细管电泳（ACE）提供了一种研究蛋白质-配体相互作用的新方法。ACE的基础是蛋白质与其配体形成复合物时其电泳迁移率的变化。可以直接对带电荷的配体定量该结合相互作用，或与先前表征的带电荷的配体竞争间接对中性配体进行定量。使用ACE确定动力学常数和平衡常数仅取决于蛋白质的迁移时间和峰形（而不是峰面积）的变化。在ACE条件下对蛋白质迁移率的模拟表明，实验获得的电泳图可以用以下几个变量来解释：打开和关闭的速率（因此，结合常数），配体的浓度，

  DOI：

  10.1021/jm00053a016

文献信息

• Using Ion Channel-Forming Peptides to Quantify Protein−Ligand Interactions
  作者：Michael Mayer、Vincent Semetey、Irina Gitlin、Jerry Yang、George M. Whitesides

  DOI：10.1021/ja077555f

  日期：2008.1.30

  This paper proposes a method for sensing affinity interactions by triggering disruption of self-assembly of ion channel-forming peptides in planar lipid bilayers. It shows that the binding of a derivative of alamethicin carrying a covalently attached sulfonamide ligand to carbonic anhydrase II (CA II) resulted in the inhibition of ion channel conductance through the bilayer. We propose that the binding

  本文提出了一种通过触发平面脂质双层中离子通道形成肽的自组装的破坏来感知亲和相互作用的方法。它表明携带共价连接的磺酰胺配体的阿拉米辛衍生物与碳酸酐酶 II (CA II) 的结合导致通过双层的离子通道电导受到抑制。我们建议庞大的 CA II 蛋白（MW 大约 30 kD）与离子通道形成肽（MW 大约 2.5 kD）的结合降低了这些肽自组装成孔的趋势或从双层中提取它们共。在这两种结果中，蛋白质和配体之间的相互作用导致自组装孔的破坏。添加竞争性抑制剂，4-羧基苯磺酰胺，到溶液中从阿拉米霉素-磺酰胺偶联物释放 CA II，并通过允许双层中离子通道的重新组装来恢复穿过双层的电流。电流在离散时间间隔内的时间平均记录使得量化这种单价配体结合相互作用成为可能。这种方法给出了大约 2 microM 的解离常数，用于在双层记录室中将 CA II 与丙氨蝶呤磺酰胺结合：该值与通过等温滴定量热法独立使用 CA II
• Dependence of Effective Molarity on Linker Length for an Intramolecular Protein−Ligand System
  作者：Vijay M. Krishnamurthy、Vincent Semetey、Paul J. Bracher、Nan Shen、George M. Whitesides

  DOI：10.1021/ja066780e

  日期：2007.2.1

  This paper reports dissociation constants and "effective molarities" (M-eff) for the intramolecular binding of a ligand covalently attached to the surface of a protein by oligo(ethylene glycol) (EG(n)) linkers of different lengths (n = 0, 2, 5, 10, and 20) and compares these experimental values with theoretical estimates from polymer theory. As expected, the value of M-eff is lowest when the linker is too short (n = 0) to allow the ligand to bind noncovalently at the active site of the protein without strain, is highest when the linker is the optimal length (n = 2) to allow such binding to occur, and decreases monotonically as the length increases past this optimal value (but only by a factor of similar to 8 from n = 2 to n = 20). These experimental results are not compatible with a model in which the single bonds of the linker are completely restricted when the ligand has bound noncovalently to the active site of the protein, but they are quantitatively compatible with a model that treats the linker as a random-coil polymer. Calorimetry revealed that enthalpic interactions between the linker and the protein are not important in determining the thermodynamics of the system. Taken together, these results suggest that the manifestation of the linker in the thermodynamics of binding is exclusively entropic. The values of M-eff are, theoretically, intrinsic properties of the EG(n) linkers and can be used to predict the avidities of multivalent ligands with these linkers for multivalent proteins. The weak dependence of M-eff on linker length suggests that multivalent ligands containing flexible linkers that are longer than the spacing between the binding sites of a multivalent protein will be effective in binding, and that the use of flexible linkers with lengths somewhat greater than the optimal distance between binding sites is a justifiable strategy for the design of multivalent ligands.
• Use of affinity capillary electrophoresis to determine kinetic and equilibrium constants for binding of arylsulfonamides to bovine carbonic anhydrase
  作者：Luis Z. Avila、Yen Ho Chu、Erich C. Blossey、George M. Whitesides

  DOI：10.1021/jm00053a016

  日期：1993.1

  Determination of kinetic and equilibrium constants using ACE relies only on the changes in the migration time and shape (but not the area) of the peak due to protein. Simulation of the protein mobility under conditions of ACE suggests that the experimentally obtained electropherograms can be explained in terms of few variables: on and off rates (and thus, binding constant), concentration of the ligand(s)

  亲和毛细管电泳（ACE）提供了一种研究蛋白质-配体相互作用的新方法。ACE的基础是蛋白质与其配体形成复合物时其电泳迁移率的变化。可以直接对带电荷的配体定量该结合相互作用，或与先前表征的带电荷的配体竞争间接对中性配体进行定量。使用ACE确定动力学常数和平衡常数仅取决于蛋白质的迁移时间和峰形（而不是峰面积）的变化。在ACE条件下对蛋白质迁移率的模拟表明，实验获得的电泳图可以用以下几个变量来解释：打开和关闭的速率（因此，结合常数），配体的浓度，
• Determination of Binding Constants of Ligands to Proteins by Affinity Capillary Electrophoresis: Compensation for Electroosmotic Flow
  作者：Frank A. Gomez、Luis Z. Avila、Yen-Ho. Chu、George M. Whitesides

  DOI：10.1021/ac00083a003

  日期：1994.6.1

  describes the estimation of binding constants (Kb) between carbonic anhydrase B (CAB, EC 4.2.1.1, from bovine erythrocytes) and charged benzenesulfonamides by affinity capillary electrophoresis (ACE) under conditions in which the migration time is affected by changes in electroosmotic flow and by nonspecific interactions accompanying changes in the concentration of ligand. Comparisons of values of migration

  本文描述了在迁移时间受电渗变化影响的条件下，亲和毛细管电泳（ACE）对碳酸酐酶B（CAB，EC 4.2.1.1，来自牛红细胞）和带电荷的苯磺酰胺之间的结合常数（Kb）的估计。流动和通过非特异性相互作用伴随配体浓度的变化。目的蛋白和“非相互作用”标记蛋白与中性内标物的迁移时间值的比较为校正可变的电渗流提供了基础。即使存在电渗流量的巨大变化，这些修正也可以估算Kb及其不确定性。