[Determination of binding domains of paeonol on immobilized human serum albumin by high-performance affinity chromatography].
High-performance affinity chromatography was used to investigate the binding of paeonol (PAE) to immobilized human serum albumin (HSA) under the condition of pH 7.4 and temperature of 37 degrees C. Self-competition zonal elution indicated that there was only one major binding site on HSA for PAE. The association constant of PAE with HSA was 4.84 x 10(3) L/mol. Competition studies based on zonal elution were carried out between PAE and various probes which have been known to interact with several major and minor sites on HSA. PAE was found to have direct competition with L-tryptophan. The results indicated that PAE interacted with Sudlow site II on HSA. The thermodynamic analysis indicated that the main force between the paeonol and HSA was hydrogen bond or van der Waals force.
Key Laboratory of Synthetic and Natural Function Molecule Chemistry of Ministry of Education, College of Chemistry & Material Science, Northwest University, Xi'an 710069, China.
Xue
X
Yu
Juncai
J
Zhang
Yinmao
Y
Wei
D000098:Acetophenones / Q000032:analysis*; D001665:Binding Sites; D002851:Chromatography, High Pressure Liquid / Q000379:methods*; D006801:Humans; D055767:Immobilized Proteins / Q000737:chemistry*; D011485:Protein Binding; D012709:Serum Albumin / Q000737:chemistry*
D000098:Acetophenones; D055767:Immobilized Proteins; D012709:Serum Albumin; C013638:paeonol