morin-5'-sulfonic acid sodium salt | 79400-76-3

• 分子结构分类: 有机化合物 - 苯丙烷和聚酮 - 黄酮类化合物
• 英文名称: morin-5'-sulfonic acid sodium salt
• 英文别名: Sodium;2-(2,4-dihydroxy-5-sulfophenyl)-3,5-dihydroxy-4-oxochromen-7-olate；sodium;2-(2,4-dihydroxy-5-sulfophenyl)-3,5-dihydroxy-4-oxochromen-7-olate
• CAS: 79400-76-3
• 化学式: C₁₅H₉O₁₀S*Na
• 分子量: 404.286
• InChiKey: UDDDGHSAXDBQTL-UHFFFAOYSA-M

计算性质

• 辛醇/水分配系数(LogP)：
  -2.39
• 重原子数：
  27
• 可旋转键数：
  2
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  193
• 氢给体数：
  5
• 氢受体数：
  10

反应信息

• 作为反应物：
  描述：

  lead(II) nitrate 、 morin-5'-sulfonic acid sodium salt 在 sodium hydroxide 、 高氯酸 作用下， 以 水 为溶剂， 生成 lead morin-5'-sulfonate complex
  参考文献：
  名称：

  Bujonek; Kopacz; Novak, Russian Journal of General Chemistry, 1996, vol. 66, # 7, p. 1037 - 1039

  摘要：

  DOI：
• 作为产物：
  描述：

  桑色素 在 硫酸 作用下， 反应 4.0h， 以50%的产率得到morin-5'-sulfonic acid sodium salt
  参考文献：
  名称：

  Study on the interaction of sodium morin-5-sulfonate with bovine serum albumin by spectroscopic techniques

  摘要：

  In the present investigation, an attempt has been made to study the interaction of sodium morin-5-sulfonate (NaMSA) with the transport proteins, bovine serum albumin (BSA) employing UV-vis, fluorometric and circular clichroism (CD) techniques. The experimental results indicated that the quenching mechanism of BSA by the compound was a static procedure. Various binding parameters were evaluated. The negative value of Delta H, positive value of Delta S and the negative value of Delta G indicated that electrostatic interactions and hydrogen bonding play major roles in the binding of the NaMSA and BSA. Based on the Forster's theory of non-radiation energy transfer, the binding distance, r, between the donor (BSA) and acceptor (NaMSA) was evaluated. The results of CD and UV-vis spectroscopy showed that the binding of this complex to BSA induces some conformational changes in BSA. (C) 2011 Elsevier B.V. All rights reserved.

  DOI：

  10.1016/j.saa.2011.10.023

文献信息

• Kopacz; Nowak; Kuznyar, Russian Journal of Inorganic Chemistry, 2002, vol. 47, # 9, p. 1344 - 1347
  作者：Kopacz、Nowak、Kuznyar、Wožnicka、Kopacz

  DOI：——

  日期：——
• Bujonek; Kopacz; Novak, Russian Journal of General Chemistry, 1996, vol. 66, # 7, p. 1037 - 1039
  作者：Bujonek、Kopacz、Novak

  DOI：——

  日期：——
• Study on the interaction of sodium morin-5-sulfonate with bovine serum albumin by spectroscopic techniques
  作者：Nahid Shahabadi、Mahnaz Mohammadpour

  DOI：10.1016/j.saa.2011.10.023

  日期：2012.2

  In the present investigation, an attempt has been made to study the interaction of sodium morin-5-sulfonate (NaMSA) with the transport proteins, bovine serum albumin (BSA) employing UV-vis, fluorometric and circular clichroism (CD) techniques. The experimental results indicated that the quenching mechanism of BSA by the compound was a static procedure. Various binding parameters were evaluated. The negative value of Delta H, positive value of Delta S and the negative value of Delta G indicated that electrostatic interactions and hydrogen bonding play major roles in the binding of the NaMSA and BSA. Based on the Forster's theory of non-radiation energy transfer, the binding distance, r, between the donor (BSA) and acceptor (NaMSA) was evaluated. The results of CD and UV-vis spectroscopy showed that the binding of this complex to BSA induces some conformational changes in BSA. (C) 2011 Elsevier B.V. All rights reserved.