4-(4-{[β-D-glucopyranosyl]sulfinylmethyl}-1-H-1,2,3-triazol-1-yl)benzenesulfonamide | 1159102-05-2

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: 4-(4-{[β-D-glucopyranosyl]sulfinylmethyl}-1-H-1,2,3-triazol-1-yl)benzenesulfonamide
• 英文别名: 4-[4-[[(2S,3R,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]sulfinylmethyl]triazol-1-yl]benzenesulfonamide
• CAS: 1159102-05-2
• 化学式: C₁₅H₂₀N₄O₈S₂
• 分子量: 448.478
• InChiKey: ZEGZELDRYWOPRH-QJFGALSTSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -2.7
• 重原子数：
  29
• 可旋转键数：
  6
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.47
• 拓扑面积：
  226
• 氢给体数：
  5
• 氢受体数：
  12

反应信息

• 作为产物：
  描述：

  4-(4-{[2',3',4',6'-tetra-O-acetyl-β-D-glucopyranosyl]sulfinylmethyl}-1-H-1,2,3-triazol-1-yl)benzenesulfonamide 在 sodium methylate 作用下， 以 甲醇 为溶剂， 以100%的产率得到4-(4-{[β-D-glucopyranosyl]sulfinylmethyl}-1-H-1,2,3-triazol-1-yl)benzenesulfonamide
  参考文献：
  名称：

  Inhibition of carbonic anhydrase isozymes with benzene sulfonamides incorporating thio, sulfinyl and sulfonyl glycoside moieties

  摘要：

  A series of benzene sulfonamides incorporating thio, sulfinyl or sulfonyl glycoside moieties were synthesized. These glycoconjugates were investigated for their ability to inhibit the enzymatic activity of four human carbonic anhydrases (hCA): isozymes I, II and tumour-associated isozymes IX and XII. The oxidation state of the sulfur in the carbohydrate tail moiety did not influence either enzyme inhibition potency or isozyme selectivity even though presenting opportunities for differing interactions with the target isozymes. (c) 2009 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2009.02.086

文献信息

• Inhibition of carbonic anhydrase isozymes with benzene sulfonamides incorporating thio, sulfinyl and sulfonyl glycoside moieties
  作者：Mathilde Singer、Marie Lopez、Laurent F. Bornaghi、Alessio Innocenti、Daniela Vullo、Claudiu T. Supuran、Sally-Ann Poulsen

  DOI：10.1016/j.bmcl.2009.02.086

  日期：2009.4

  A series of benzene sulfonamides incorporating thio, sulfinyl or sulfonyl glycoside moieties were synthesized. These glycoconjugates were investigated for their ability to inhibit the enzymatic activity of four human carbonic anhydrases (hCA): isozymes I, II and tumour-associated isozymes IX and XII. The oxidation state of the sulfur in the carbohydrate tail moiety did not influence either enzyme inhibition potency or isozyme selectivity even though presenting opportunities for differing interactions with the target isozymes. (c) 2009 Elsevier Ltd. All rights reserved.