化学学报 ›› 2004, Vol. 62 ›› Issue (16): 1460-1466. 上一篇    下一篇

研究论文

β-1,2,3,4,6-五-O-倍酰-D-葡萄糖与人血清白蛋白的相互作用研究

谢孟峡, 蒋敏, 李崧, 刘媛   

  1. 北京师范大学分析测试中心, 北京, 100875
  • 投稿日期:2004-02-03 修回日期:2004-04-20 发布日期:2014-02-17
  • 通讯作者: mengxia-xie@263.net
  • 作者简介:谢孟峡,E-mail:mengxia-xie@263.net

Study on the Interaction of β-1,2,3,4,6-Penta- O-galloyl- D-glucopyranose with Human Serum Albumin

XIE Meng-Xia, JIANG Min, LI Song, LIU Yuan   

  1. Analytical & Testing Center of Beijing Normal University, Beijing 100875
  • Received:2004-02-03 Revised:2004-04-20 Published:2014-02-17

应用红外光谱和荧光光谱方法研究了人血清白蛋白(HSA)与β-1,2,3,4,6-五-O-倍酰-D-葡萄糖(PGG)的相互作用.荧光光谱结果显示,PGG在CPGG/CHSA<0.5和0.5<GPGG/CHsA<3两个浓度范围内在HSA分子上分别有一个和两个结合位点,结合常数分别为1.66吆4和8.98吆8L·mol-1.运用蛋白质红外光谱酰氨Ⅲ带和酰氨Ⅰ带结合的方法对HSA与PGG作用后二级结构的变化进行了定量分析.随着药物浓度的增加,PGG和HSA之间的相互作用主要使HSA的二级结构发生了由α-螺旋向β-转角和无规结构的转化.结合荧光光谱和红外光谱结果,探讨了HSA与不同浓度PGG作用引起的荧光猝灭与二级结构变化之间的关系,并讨论了HSA和PGG相互作用的模式.

关键词: β-1,2,3,4,6-五-O-倍酰-D-葡萄糖, 人血清白蛋白, 傅立叶变换红外光谱, 荧光光谱, 二级结构

Interaction of β-1,2,3,4,6-penta-O-galloyl-D-glucopyranose (PGG) with human serum albumin (HSA) has been studied by Fourier transform infrared (FT-IR) and fluorescence spectroscopic methods.Fluorescence data revealed the presence of one binding site on HSA when CPGG/CHSA<0.5, and two sites when 0.5<CPGG/CHSA<3.The binding constants (KA) are 1 66吆 4 and 8 98吆 8 L·mol -1 in the two concentration ranges respectively.The changes of the secondary structure of HSA after interacting with PGG were estimated by combining the curve-fitting results of amide Ⅰ and amide Ⅲ bands of the protein infrared spectra.It was found that with the increase of PGG concentration, the interaction of PGG with HSA has mainly caused the change from the α-helix structure to β-turn and random coil structure.Combining the results of fluorescence and FT-IR, the relationship of fluorescence quenching and the changes of HSA secondary structure induced by PGG binding was investigated, and the PGG-HSA interaction mode was discussed.

Key words: β-1,2,3,4,6-penta-O-galloyl-D-glucopyranose, human serum albumin, FT-IR, fluorescence, secondary structure