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Binding of caffeic acid to human serum albumin by the retention data and frontal analysis
Author(s) -
An Yuxin,
Li Qian,
Chen Jiejun,
Gao Xiaokang,
Chen Hongwei,
Xiao Chaoni,
Bian Liujiao,
Zheng Jianbin,
Zhao Xinfeng,
Zheng Xiaohui
Publication year - 2014
Publication title -
biomedical chromatography
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.4
H-Index - 65
eISSN - 1099-0801
pISSN - 0269-3879
DOI - 10.1002/bmc.3238
Subject(s) - chemistry , chromatography , caffeic acid , albumin , serum albumin , human serum albumin , biochemistry , antioxidant
A new mathematical model and frontal analysis were used to characterize the binding behavior of caffeic acid to human serum albumin (HSA) based on high‐performance affinity chromatography. The experiments were carried out by injecting various mole amounts of the drug onto an immobilized HSA column. They indicated that caffeic acid has only one type of binding site to HSA on which the association constant was 2.75 × 10 4 / m . The number of the binding site involving the interaction between caffeic acid and HSA was 69 n m . The data obtained by the frontal analysis appeared to present the same results for both the association constant and the number of binding sites. This new model based on the relationship between the mole amounts of injection and capacity factors assists understanding of drug–protein interaction. The proposed model also has the advantages of ligand saving and rapid operation. Copyright © 2014 John Wiley & Sons, Ltd.