首页 | 本学科首页   官方微博 | 高级检索  
   检索      


Multispectroscopic studies of the interaction of folic acid with glycated human serum albumin
Authors:Urszula ?liwińska-Hill  Katarzyna Wiglusz
Institution:1. Department of Analytical Chemistry, Faculty of Pharmacy, Wroclaw Medical University, Wroc?aw, Polandurszula.sliwinska-hill@umed.wroc.pl;3. Department of Analytical Chemistry, Faculty of Pharmacy, Wroclaw Medical University, Wroc?aw, Poland
Abstract:Abstract

The interaction between glycated human serum albumin (gHSA) and folic acid (FA) was investigated by various spectroscopic techniques, such as fluorescence, circular dichroism, UV–vis absorption spectroscopy and electrophoretic light scattering technique. These methods characterize the binding properties of an albumin–folic acid system. The binding constants values (Ka) at 300 and 310 K are about 104 M?1. The standard enthalpy change (ΔH) and the standard entropy change (ΔS) were calculated to be ~?20?kJ mol?1 and ~16 J mol?1 K?1, respectively, which indicate characteristic electrostatic interactions between gHSA and folic acid. The CD studies showed that there are no significant conformational changes in the secondary structure of the protein. Moreover, the zeta potential measurements proved that under physiological conditions the gHSA–folic acid complex shows instability. No significant changes in the secondary structure of the protein and reversible drug binding are the desirable effect from pharmacological point of view.

Communicated by Ramaswamy H. Sarma
Keywords:circular dichroism (CD)  glycated human serum albumin  fluorescence quenching  folic acid  zeta potential and electrophoretic light scattering (ELS)
设为首页 | 免责声明 | 关于勤云 | 加入收藏

Copyright©北京勤云科技发展有限公司  京ICP备09084417号