芦丁与人血清白蛋白相互作用的紫外可见光谱特性研究

摘要

In order to inveatigate the interaction between rutin and human serum albumin (lISA) ,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 ～23.0 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 fluoresenee of HSA is also influenced by mtin. The excitation wavelength will be shift towards long wavelength, while emission wavelength will be shift towards short wavelength when HSA interacted with rutin.%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354.5nm)、在330～300nm及300～230nm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.