Journal
FOOD CHEMISTRY
Volume 372, Issue -, Pages -Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2021.131280
Keywords
Gingerols; Bovine serum albumins; Fluorescence; Molecular modelling; Binding interaction
Funding
- S&T projects of Guangdong Province [2019B020212004]
- 111 Project [B17018]
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The study found that gingerols can form stable complexes with BSA, significantly improving their solubility and stability. By binding with BSA, gingerols enhanced their solubility and antioxidant capacity, providing a promising strategy for enhancing the bioavailability and efficacy of gingerols.
In this study, the binding mechanism between bovine serum albumin (BSA) and three gingerols ([6]-, [8]- and [10]-gingerol) was evaluated to explore an effective strategy for improving solubility and stability of gingerols. The fluorescence analysis suggested gingerols could bind with BSA to form a stable BSA/gingerols complex and [10]-gingerol had the strongest binding affinity (Ka = 4.016 x 104 L/mol) at 298 K. Thermodynamic parameters and molecular modeling validated that hydrophobic interaction and hydrogen bonds were the main driving force for the interaction of BSA/gingerols. Gingerols bound to BSA at site I (subdomain IIA) resulted in a conformational change of BSA with a structure shrinkage, which was responsible for the decrease of surface hydrophobicity. The formation of BSA/gingerols complexes promoted the solubility of [6]-, [8]- and [10]-gingerol increasing by 1.50, 6.04 and 23.50 times, respectively. In addition, the stability and antioxidant capacity of gingerols was significantly improved after binding with BSA.
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