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Characterization of polyunsaturated fatty acid binding to albumin using isothermal titration calorimetry
Author(s) -
Niu ShuiLin,
Culyba Elizabeth,
Mitchell Drake C.
Publication year - 2007
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.21.6.a981-d
Subject(s) - isothermal titration calorimetry , polyunsaturated fatty acid , chemistry , human serum albumin , titration , fatty acid binding protein , binding site , lauric acid , chromatography , fatty acid , biochemistry , organic chemistry , gene
Objective: Polyunsaturated fatty acids (PUFA) are highly enriched in the central nervous system and are essential for proper brain development and function. Human serum albumin (HSA) is a major fatty acid (FA) binding protein in plasma that is responsible for the transport and utilization of PUFA. The current knowledge of PUFA binding to HSA is limited. Previous studies on FA binding to HSA were focused on saturated or monounsaturated FA and the results were widely varied. This study aimed to characterize PUFA binding to HSA using a new method. Methods: Isothermal titration calorimetry is a powerful technique to determine the thermodynamics of molecular binding by measuring the heat signal evolved from the binding event. An aliquot of PUFA was titrated into HSA or vise versa, until the binding event reached saturation. The binding isotherm was analyzed using the Scatchard and Sequential Binding models to derive the binding parameters. Results & Conclusion: The titration of PUFA to HSA produced a series of well‐resolved exothermic peaks. A total of 11 binding sites were resolved from the binding isotherm. The binding constants and binding free energies were determined for the first time for a series of PUFA. Such findings will provide insights into the physiology of transport and utilization of PUFA.