houpulin B

• 分子结构分类: 有机化合物 - 苯类化合物 - 酚类
• 英文名称: houpulin B
• 化学式: C₃₆H₃₄O₄
• 分子量: 530.664
• InChiKey: HDYLDMBBQBLCRI-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  8.42
• 重原子数：
  40.0
• 可旋转键数：
  11.0
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.11
• 拓扑面积：
  80.92
• 氢给体数：
  4.0
• 氢受体数：
  4.0

上下游信息

• 上游原料

  中文名称	英文名称	CAS号	化学式	分子量
  和厚朴酚	Honokiol	35354-74-6	C18H18O2	266.34

反应信息

• 作为产物：
  描述：

  和厚朴酚 在 双氧水 、 Momordica charantia peroxidase 作用下， 以 丙酮 为溶剂， 反应 12.0h， 以6 mg的产率得到3',3''',3''''',5,5'',5''''-hexaallyl-[1,1':5',1'':3'',1''':5''',1'''':3'''',1'''''-sexiphenyl]-2,2'',2'''',4',4''',4'''''-hexol
  参考文献：
  名称：

  Honokiol trimers and dimers via biotransformation catalyzed by Momordica charantia peroxidase: Novel and potent α-glucosidase inhibitors

  摘要：

  Ten honokiol oligomers (1-10), including four novel trimers (1-4) and four novel dimers (5-8), were obtained by means of biotransformation of honokiol catalyzed by Momordica charantia peroxidase (MCP) for the first time. Their structures were established on the basis of spectroscopic methods. The biological results demonstrated that most of the oligomers were capable of inhibiting alpha-glucosidase with significant abilities, which were one to two orders of magnitude more potent than the substrate, honokiol. In particular, compound 2, the honokiol trimer, displayed the greatest inhibitory activity against alpha-glucosidase with an IC50 value of 1.38 mu M. Kinetic and CD studies indicated that 2 inhibited alpha-glucosidase in a reversible, mixed-type manner and caused conformational changes in the secondary structure of the enzyme protein. These findings suggested that 2 might be exploited as a promising drug candidate for the treatment of diabetes. (C) 2013 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2013.12.005

文献信息

• Honokiol trimers and dimers via biotransformation catalyzed by Momordica charantia peroxidase: Novel and potent α-glucosidase inhibitors
  作者：Ye He、Xiao-Bing Wang、Bo-Yi Fan、Ling-Yi Kong

  DOI：10.1016/j.bmc.2013.12.005

  日期：2014.1

  Ten honokiol oligomers (1-10), including four novel trimers (1-4) and four novel dimers (5-8), were obtained by means of biotransformation of honokiol catalyzed by Momordica charantia peroxidase (MCP) for the first time. Their structures were established on the basis of spectroscopic methods. The biological results demonstrated that most of the oligomers were capable of inhibiting alpha-glucosidase with significant abilities, which were one to two orders of magnitude more potent than the substrate, honokiol. In particular, compound 2, the honokiol trimer, displayed the greatest inhibitory activity against alpha-glucosidase with an IC50 value of 1.38 mu M. Kinetic and CD studies indicated that 2 inhibited alpha-glucosidase in a reversible, mixed-type manner and caused conformational changes in the secondary structure of the enzyme protein. These findings suggested that 2 might be exploited as a promising drug candidate for the treatment of diabetes. (C) 2013 Elsevier Ltd. All rights reserved.