Rapid determination of protein binding constant by a pressure-mediated affinity capillary electrophoresis method

被引：22

作者：

Zhang, Bo ^{[1
]}

Li, You X. ^{[1
]}

Gao, He N. ^{[1
]}

Bian, Juan ^{[1
]}

Bao, James J. ^{[1
]}

机构：

[1] Tianjin Univ, Sch Pharmaceut Sci & Technol, Tianjin Key Lab Modem Drug Delivery & High Effici, Tianjin 300072, Peoples R China

来源：

ELECTROPHORESIS | 2011年 / 32卷 / 24期

基金：

中国国家自然科学基金;

关键词：

Affinity capillary electrophoresis; Binding constant; Mobility determination; Pressure-mediated electrophoresis; Protein; HUMAN SERUM-ALBUMIN; DRUG-BINDING; FRONTAL ANALYSIS; MIGRATION TIME; PROPAFENONE; PERFORMANCE; MOBILITY; REPRODUCIBILITY; CHROMATOGRAPHY; DIALYSIS;

D O I：

10.1002/elps.201100211

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

A new pressure-mediated affinity capillary electrophoresis method for the rapid and accurate determination of drugprotein binding constants is described. A special combination of pressure and electrophoresis is used to shorten the electrophoresis and the overall analysis time to only a few minutes. At the same time, the suitability of this method is checked against a traditional fluorescence spectroscopy method. The binding constants of bovine serum albumin and a total of eight drugs with different pKa have been evaluated and compared with those determined by the fluorescence spectroscopy method and other methods in literature. The results indicate that the P-ACE method is well suited for the determination of binding constants with weak interaction (Kb<105?M-1).

引用

页码：3589 / 3596

页数：8

共 45 条

[1] Drug binding to human serum albumin: Abridged review of results obtained with high-performance liquid chromatography and circular dichroism [J].