Effect of interaction between resveratrol and myofibrillar protein on the production of bound heterocyclic amines

Abstract

To elucidate the pathways and mechanisms by which polyphenols inhibit protein-bound heterocyclic amines (HAs), the influence of resveratrol on bound/free HAs and the structure changes of myofibrillar proteins (MP) in the system of creatinine/MP/glucose model was studied. The results demonstrate that resveratrol significantly reduced bound and free HAs in the reaction systems (P < 0.05), and facilitates the transition from bound to free HAs. In addition, resveratrol altered the secondary structure of MP and had a static quenching effect on MP fluorescence. The strong interactions between resveratrol and MP are mainly hydrogen bonding and hydrophobic interactions. Furthermore, the results of molecular docking demonstrated that resveratrol exposed more hydrophobic amino acids (Ala, Lys and Pro) at the 556–578 amino acid sites of myosin. These results indicate that resveratrol controls the formation of bound HAs by reducing exposure to amino acids involved in the HAs reaction and promoting exposure to non-precursor amino acids.