2,3,4,6-tetra-O-acetyl-β-D-sulfinylpropynylglucopyranoside | 1159101-94-6

• 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: 2,3,4,6-tetra-O-acetyl-β-D-sulfinylpropynylglucopyranoside
• CAS: 1159101-94-6
• 化学式: C₁₇H₂₂O₁₀S
• 分子量: 418.422
• InChiKey: PWOIXCCKNXHCND-YADRHWFLSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.55
• 重原子数：
  28.0
• 可旋转键数：
  7.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.65
• 拓扑面积：
  131.5
• 氢给体数：
  0.0
• 氢受体数：
  10.0

反应信息

• 作为反应物：
  描述：

  2,3,4,6-tetra-O-acetyl-β-D-sulfinylpropynylglucopyranoside 、 4-azidobenzenesulfonamide 在 copper(ll) sulfate pentahydrate 、 sodium ascorbate 作用下， 以 乙醇 、 水 为溶剂， 反应 2.0h， 以45%的产率得到4-(4-{[2',3',4',6'-tetra-O-acetyl-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
• 作为产物：
  描述：

  2-propynyl 2,3,4,6-tetra-O-acetyl-β-D-1-thioglucopyranoside 在 间氯过氧苯甲酸 作用下， 以 二氯甲烷 为溶剂， 以70%的产率得到2,3,4,6-tetra-O-acetyl-β-D-sulfinylpropynylglucopyranoside
  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