Fatty acids (FAs) are transported by serum albumin in plasma. Studies have been undertaken to address the binding of MCFAs or LCFAs to human plasma albumin (HPA) and bovine serum albumin (BSA) by characterizing the binding affinities. Previous research on FA binding to serum albumin was usually performed in dilute solutions that are not sufficiently concentrated for the interpretation of the significance of the results under normal physiological conditions. How macromolecular crowded media affect fatty acids and bovine serum albumin (BSA) binding remains unknown. In this article, we investigated the mechanism of FA-BSA binding in a polyethylene glycol crowding environment by using thermodynamic and spectroscopic methods. Molecular crowding increased the binding constant for saturated medium-chain fatty acids (MCFAs) but significantly decreased the binding constant for unsaturated long-chain FAs. The binding sites tended to increase in all the cases. Further investigation revealed that crowding media might loosen the structure of BSA, facilitating MCFA-BSA binding. This research is useful for understanding the transportation of FAs by BSA under physiological conditions and may also help to control digestion by the eventual incorporation of macromolecular crowding agents into food formulations.

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