Behavior of interacting species in vacancy affinity capillary electrophoresis described by mass balance equation

被引:10
|
作者
Sun, Ying [1 ]
Fang, Ning [2 ]
Chen, David D. Y. [1 ]
机构
[1] Univ British Columbia, Dept Chem, Vancouver, BC V6T 1Z1, Canada
[2] Iowa State Univ, Dept Chem, Ames, IA 50011 USA
基金
加拿大自然科学与工程研究理事会;
关键词
affinity capillary electrophoresis; binding constant; mass balance equation; vacancy affinity capillary electrophoresis;
D O I
10.1002/elps.200800206
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Vacancy ACE (VACE) is one of the ACE methods, and has been used to study binding interactions between different biomolecules. Thermodynamic binding constants can be estimated with nonlinear regression methods. With a highly efficient computer simulation program (SimDCCE), it is possible to demonstrate the detailed behaviors of each species during the interaction process under different conditions. In this work, thirteen scenarios in four different combinations of migration orders of the free protein, free drug, and complex formed are studied. The detailed interaction process between protein and ligand is discussed and illustrated based on the mass balance equation, also called mass transfer equation. By properly setting the parameters in the simulation model, the influence of different factors during the interaction process can be well understood.
引用
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页码:3333 / 3341
页数:9
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