Characterization of bovine serum albumin-tryptophan interaction by capillary isoelectric focusing with whole column imaging detection
Characterization of bovine serum albumin-tryptophan interaction by capillary isoelectric focusing with whole column imaging detection
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DOI：
10.1016/j.chroma.2005.08.092
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发表时间：
2006-02-10
影响因子：
4.1
通讯作者：
Pawliszyn, J
中科院分区：
文献类型：
--
作者：
Bo, T;Pawliszyn, J
Capillary isoelectric focusing (cIEF) with whole column imaging detection (WCID) was explored for the characterization of bovine serum albumin (BSA)-tryptophan interaction, to further understand protein-drug interactions. The BSA-tryptophan interaction was dynamically monitored by cIEF-WCID, to provide the cIEF profiles of the BSA-tryptophan interaction system at different focusing times. Our study demonstrated that the cIEF behavior of BSA can serve as a probe into the study of BSA-tryptophan interaction, through monitoring the change in its cIEF profile when the interaction occurred. The study illustrated that the BSA peak split due to the BSA-tryptophan interaction, and the peak of BSA-tryptophan complex was clearly identified in the cIEF electropherograms. By comparing the cIEF profiles of BSA/L-tryptophan and BSA/D-tryptophan, respectively, our study demonstrated that BSA interacted with the enantiomers of tryptophan with a chiral recognition. L-Tryptophan demonstrated a very strong interaction with BSA, while D-tryptophan exhibited a much weaker interaction with BSA. The effects of the BSA concentration, the tryptophan concentration, the focusing time and the incubation time on the BSA-tryptophan interaction were investigated. This study offers a novel approach for the study of protein-drug interactions. (c) 2005 Elsevier B.V. All rights reserved.
