Dual suppression of heterocyclic amines and advanced glycation end products via glucosinolate-myosin binding: Spectroscopic and computational elucidation

The present research evaluated the effects of two glucosinolates (sinigrin and glucobrassicin) derived from Armoracia rusticana on structural alterations, antioxidant capacity of myosin, and accumulation of heterocyclic amine (HAs) and advanced glycation end products (AGEs). Experimental assays, quantum chemical computations, and molecular dynamics simulations were combined to systematically unravel the structure-function mechanism by which glucosinolates modulate myosin. Results showed that glucosinolates bound to myosin via static quenching, inducing conformational changes that enhanced myosin’s antioxidant capacity, delayed peroxidation, and ultimately suppressed the formation of HAs and AGEs. Notably, quantum chemical computations demonstrated that glucobrassicin possessed a smaller energy gap than sinigrin, indicating superior free radical scavenging and binding capabilities; molecular dynamics simulations further identified stable binding of glucobrassicin to myosin at residues Phe:247, Leu:270, and Glu:272—key sites mediating the synergistic antioxidant effect. Collectively, this work elucidates the mechanism by which glucosinolates structurally modulate myosin to enhance antioxidant capacity and mitigate the formation of HAs and AGEs, offering novel insights for supporting the application of Armoracia rusticana -derived glucosinolates as natural and safe strategies to improve the safety and health benefits of meat. • Glucosinolates bind to myosin inducing conformational changes. • Glucosinolates boost antioxidant capacity of myosin, mitigate HAs/AGEs formation. • Glucobrassicin shows stronger antioxidant and binding abilities than sinigrin. • Glucobrassicin can stably bind to residue Phe:247, Leu:270, and Glu:272 of myosin.