Comprehensive binding analysis of glycated myosin with furan derivatives via glucose by means of multi-spectroscopy techniques and molecular docking simulation

Myosin is an ideal binding receptor for aroma compounds and its functional properties are easily affected by glucose. The study comprehensively clarified the effects of glucose glycation-induced structural modifications of myosin on its binding ability with furan derivatives, including 2-methylfuran, 2-furfural , and 2-furfurylthiol. The results demonstrated that the binding levels of furan derivatives were obviously affected by the glycation levels of myosin due to the changes of myosin structure and surface. The increased glycation levels caused the unfolding of myosin structu r e and accelerated the aggregation, as were exhibited by the data of zeta potential , particle size, microstructure, and secondar y structure. The glycated myosin with wrinkled surfaces favored the significant increase of hydrophobic interactions (31.59-69.50 & mu;g), the more exposure of amino acid residues (3459-6048), the formation of free sulfhydryl groups (16.37-20.58 mmol/104g) and hydrogen bonds. These key (non)covalent linkages accounted for the generation of glycated myosin-odorants complex, including 2-furfur-ylthiol (29.17-47.87 %), thus enhancing the resultant binding ability as evidenced by the free furan de-rivatives concentrations, fluorescence quenching and molecular docking simulation analysis. The glycated myosin for 8 h bound highest concentrations of f ur a n derivatives. The results wil l provide comprehensive data on the retention of aroma compounds in meat products.

Automated summary

The study comprehensively clarified the effects of glucose glycation-induced structural modifications of myosin on its binding ability with furan derivatives, demonstrating that the binding levels of furan derivatives were obviously affected by the glycation levels of myosin due to the changes of myosin structure and surface.