Analysis of conformational change of human serum albumin using chiral capillary electrophoresis.
The conformational change of human serum albumin (HSA) was studied through its binding with basic drug-mexiletine by chiral capillary electrophoresis. The effects of the conformational change of HSA resulted from pH, thermal, acute vibration, and alcohol on its chiral selectivity to mexiletine were investigated in detail. This study offers a simple and complementary method to investigate the binding of proteins with drugs and the characteristic of conformational change of protein. The method is easy to perform, high speed, low reagent consumption, and no modification is required to the commercially available CE instrument.
Xu
Hui
H
Laboratory of Life Analytical Chemistry, Department of Chemistry, Nanjing University, Nanjing 210093, China.
Yu
Xiao-Dong
XD
Chen
Hong-Yuan
HY
D019075:Electrophoresis, Capillary / Q000379:methods*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D011487:Protein Conformation; D012709:Serum Albumin / Q000737:chemistry*; D013237:Stereoisomerism
D012709:Serum Albumin