天然产物研究与开发 ›› 2011, Vol. 23 ›› Issue (3): 476-481.

• 研究简报 • 上一篇    下一篇

芦丁与人血清白蛋白相互作用的紫外可见光谱特性研究

黄汉昌1*,姜招峰2   

  1. 1北京联合大学应用文理学院;2北京联合大学生物活性物质与功能食品北京市重点实验室,北京 100191
  • 收稿日期:2009-09-09 出版日期:2011-06-25 发布日期:2011-08-08
  • 通讯作者: hanchang@ygi.edu.cn

Interaction between Rutin and Human Serum Albumin by UV-Vis Spectrum

HUANG Han-chang1*, JIANG Zhao-feng2   

  1. 1College of Arts and Science of Beijing Union University; 2Beijing Key Laboratory of Bioactive Substances and Functional Foods of Beijing Union University, Beijing 100191, China
  • Received:2009-09-09 Online:2011-06-25 Published:2011-08-08

摘要:

本文通过测定芦丁与HSA相互作用前后的紫外可见吸收光谱、圆二色性及人血清白蛋白(HSA)的荧光特性,研究了芦丁与HSA结合作用。结果表明,芦丁在紫外区有三个特征的吸收峰(264.0、285.5及354.5 nm)、在330~300 nm及300~230 nm处显示圆二色性,HSA引起芦丁紫外可见吸收光谱波峰红移;芦丁与HSA相互作用后,不引起HSA二级结构的改变,但对其三级结构有影响,同时对HSA荧光激发及发生光谱最大峰位及幅度有影响。

Abstract:

In order to inveatigate the interaction between rutin and human serum albumin (HSA), this article determined the ultraviolt-visible (UV-Vis) absorption spectrum, circular diachroism and HSA fluorescence spectrum, and further to analyse the difference between the spectra before and after rutin and HSA mixed. The results indicated that rutin shows three particular UV absorption-peak at the wavelength 264.0, 285.5 and 354.5 nm and circular diachroism at the wavelength ranges 330~300 nm and 300~230 nm. When rutin interacted with HSA, the UV absorption peak of Rutin will be shifted to long wavelength. However, for the structure of HSA, rutin will change the HSA tertiary structure rather than secondary strcture. The fluoresence of HSA is also influenced by rutin. The excitation wavelength will be shift towards long wavelength, while emission wavelength will be shift towards short wavelength when HSA interacted with rutin.

Key words: Human Serum Albumin (HSA), UV-Vis absorption, Circular Diachroism, fluorescence

中图分类号: 

Q81