降钙素 | 493-36-7

• 分子结构分类: 有机化合物 - 苯丙烷和聚酮 - 橙酮类黄酮
• 中文名称: 降钙素
• 英文名称: alphitonin
• 英文别名: 2-[(3,4-dihydroxyphenyl)methyl]-2,4,6-trihydroxy-1-benzofuran-3-one
• CAS: 493-36-7
• 化学式: C₁₅H₁₂O₇
• 分子量: 304.256
• InChiKey: VCLACNNZBMRRES-UHFFFAOYSA-N

物化性质

• 溶解度：
  DMF：可溶； DMSO：可溶；乙醇：可溶；甲醇：可溶

计算性质

• 辛醇/水分配系数(LogP)：
  1.8
• 重原子数：
  22
• 可旋转键数：
  2
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.13
• 拓扑面积：
  127
• 氢给体数：
  5
• 氢受体数：
  7

反应信息

• 作为产物：
  描述：

  花旗松素 在 没食子酸 作用下， 以 水 为溶剂， 反应 60.0h， 生成 降钙素
  参考文献：
  名称：

  The Thermal and Enzymatic Taxifolin–Alphitonin Rearrangement

  摘要：

  This report describes a detailed investigation of the thermal and enzymatic conversion of taxifolin to alphitonin. Chromatographic separation of the four dihydroquercetin stereoisomers 1-4 in combination with circular dichroism spectroscopy permitted elucidation of the kinetics of this rearrangement and characterization of the different reaction pathways involved. Our findings are corroborated by quantum chemistry calculations that reveal a unique cascade of tautomerization processes leading from taxifolin to alphitonin and also explain the racemization of alphitonin at room temperature. Furthermore, the substrate specificity toward (+)-taxifolin of an enzyme from Eubacterium ramulus catalyzing this intriguing rearrangement is demonstrated.

  DOI：

  10.1021/np200639s

文献信息

• Chopin et al., Comptes Rendus Hebdomadaires des Seances de l'Academie des Sciences, 1964, vol. 258, p. 5231
  作者：Chopin et al.

  DOI：——

  日期：——
• Zwingelstein; Jouanneteau, Comptes Rendus Hebdomadaires des Seances de l'Academie des Sciences, 1955, vol. 240, p. 981
  作者：Zwingelstein、Jouanneteau

  DOI：——

  日期：——
• Plasma-Induced Degradation of Quercetin Associated with the Enhancement of Biological Activities
  作者：Tae Hoon Kim、Jaemin Lee、Hyun-Joo Kim、Cheorun Jo

  DOI：10.1021/acs.jafc.7b00987

  日期：2017.8.16

  Nonthermal plasma is a promising technology to improve the safety and to extend the shelf-life of various minimally processed foods. However, research on plasma-induced systemic degradation related to changes in chemical structure and biological activity is still very limited. In this study, the enhancement of biological activity and the mechanism of degradation of the most common type of flavonol, quercetin, induced by a dielectric barrier discharge (DBD) plasma were investigated. Quercetin is dissolved in methanol and exposed to nonthermal DBD plasma for 5, 10, 20, and 30 min. The quercetin treated with the plasma for 20 min showed rapidly increased alpha-glucosidase inhibitory and radical scavenging activities compared to those of parent quercetin. The structures of the degradation products 13 from the quercetin treated with the plasma for 20 min were isolated and characterized by interpretation of their spectroscopic data. Among the generated products, (+/-)-alphitonin (1) exhibited significantly improved antidiabetic and antioxidant properties compared to those of the parent quercetin. The antidiabetic and antioxidant properties were measured by alpha-glucosidase inhibition and 1,1-diphenyl-2-picrylhydrazyl radical scavenging assays. These results suggested that structural changes in quercetin induced by DBD plasma might be attributable to improving the biological activity.
• The Thermal and Enzymatic Taxifolin–Alphitonin Rearrangement
  作者：Paul W. Elsinghorst、Taner Cavlar、Anna Müller、Annett Braune、Michael Blaut、Michael Gütschow

  DOI：10.1021/np200639s

  日期：2011.10.28

  This report describes a detailed investigation of the thermal and enzymatic conversion of taxifolin to alphitonin. Chromatographic separation of the four dihydroquercetin stereoisomers 1-4 in combination with circular dichroism spectroscopy permitted elucidation of the kinetics of this rearrangement and characterization of the different reaction pathways involved. Our findings are corroborated by quantum chemistry calculations that reveal a unique cascade of tautomerization processes leading from taxifolin to alphitonin and also explain the racemization of alphitonin at room temperature. Furthermore, the substrate specificity toward (+)-taxifolin of an enzyme from Eubacterium ramulus catalyzing this intriguing rearrangement is demonstrated.