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Comparative studies of the interaction between ferulic acid and bovine serum albumin by ACE and surface plasmon resonance
Author(s) -
Zhang Yintang,
Xu Maotian,
Du Ming,
Zhou Feimeng
Publication year - 2007
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.200700025
Subject(s) - surface plasmon resonance , chemistry , bovine serum albumin , ferulic acid , capillary electrophoresis , binding constant , analytical chemistry (journal) , electrophoresis , resonance (particle physics) , chromatography , binding site , materials science , biochemistry , nanotechnology , physics , particle physics , nanoparticle
Affinity capillary electrophoresis (ACE) was used to study the interaction between ferulic acid (FA) and BSA. The interaction between FA and BSA was facilitated by injecting FA into a BSA‐containing running buffer. Both mobility ratio and mobility shift assays were performed to deduce the binding constant ( K b ). However, the K b value obtained with the mobility ratio assay was only ˜20% of that extracted from the mobility shift assay. The former assay yielded a K b value (5.6 ± 0.4×10 4 M –1 ), which compares well with the result obtained with surface plasmon resonance (SPR) (5.1 ± 0.6×10 4 M –1 ). The discrepancy between the mobility ratio and mobility shift assays suggests that the data extrapolation from the mobility ratio should be more reliable for cases when both changes in the EOF and viscosity of the running buffer are important. The work demonstrates that ACE, a solution‐based technique, and SPR, a technique addressing interfacial processes, are highly complementary to each other and the comparative studies are confirmatory and allow binding constants to be accurately determined.