5-[(Benzylamino)methyl]furan-2-sulfonic acid | 189172-49-4

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 有机磺酸及其衍生物
• 英文名称: 5-[(Benzylamino)methyl]furan-2-sulfonic acid
• CAS: 189172-49-4
• 化学式: C₁₂H₁₃NO₄S
• 分子量: 267.306
• InChiKey: XSELUGDRPCBUOQ-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -1.3
• 重原子数：
  18
• 可旋转键数：
  5
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.17
• 拓扑面积：
  87.9
• 氢给体数：
  2
• 氢受体数：
  5

反应信息

• 作为产物：
  描述：

  (5-Imino-2-sulfonic acid furane)(phenyl)methanamine 在 sodium tetrahydroborate 作用下， 以 甲醇 为溶剂， 反应 4.0h， 以46%的产率得到5-[(Benzylamino)methyl]furan-2-sulfonic acid
  参考文献：
  名称：

  Carbonic Anhydrase-Encoded Dynamic Constitutional Libraries: Toward the Discovery of Isozyme-Specific Inhibitors

  摘要：

  A constitutional dynamic library (CDL) was generated under thermodynamic control by using the amino-carbonyl/imine interconversion as reversible chemistry, combined with noncovalent bonding within the active site of the metalloenzyme carbonic anhydrase (CA, EC 4.2.1.1). Considering the pharmacological importance to find isoform-selective CA inhibitors (CAIs), two of the 15 human (h) isoform, i.e., hCAI and hCAII, have been subjected to a parallel screening of the same CDL. The use of parallel constitutional screening of CDL chemistry for the discovery of enzyme inhibitors is straightforward and it might provide initial insights toward the generation of efficient classes of selective, high affinity inhibitors. We demonstrate here that the high selectivity and specificity of inhibiting the hCAI and hCAII. isozymes with some of the detected hits may be used to describe a complex constitutional behavior through component selection from the dynamic library, driven by the selective binding to the specific isoform active site. These results also point to the possibility of modulating the drug discovery methods by constitutional recomposition induced by a specific enzymatic target.

  DOI：

  10.1021/jm900449v

文献信息

• Carbonic Anhydrase-Encoded Dynamic Constitutional Libraries: Toward the Discovery of Isozyme-Specific Inhibitors
  作者：Gihane Nasr、Eddy Petit、Daniela Vullo、Jean-Yves Winum、Claudiu T. Supuran、Mihail Barboiu

  DOI：10.1021/jm900449v

  日期：2009.8.13

  A constitutional dynamic library (CDL) was generated under thermodynamic control by using the amino-carbonyl/imine interconversion as reversible chemistry, combined with noncovalent bonding within the active site of the metalloenzyme carbonic anhydrase (CA, EC 4.2.1.1). Considering the pharmacological importance to find isoform-selective CA inhibitors (CAIs), two of the 15 human (h) isoform, i.e., hCAI and hCAII, have been subjected to a parallel screening of the same CDL. The use of parallel constitutional screening of CDL chemistry for the discovery of enzyme inhibitors is straightforward and it might provide initial insights toward the generation of efficient classes of selective, high affinity inhibitors. We demonstrate here that the high selectivity and specificity of inhibiting the hCAI and hCAII. isozymes with some of the detected hits may be used to describe a complex constitutional behavior through component selection from the dynamic library, driven by the selective binding to the specific isoform active site. These results also point to the possibility of modulating the drug discovery methods by constitutional recomposition induced by a specific enzymatic target.