Combined computational and spectroscopic analyses of the interactions between ginger compounds and bovine type I collagen.

The stability of collagen is critical for meat quality; however, how ginger compounds act as collagen stabilizers is poorly understood. Molecular docking identified 24 compounds with binding affinities below -5.0 kcal/mol, involving Pro168, Tyr161, and Arg179 as key residues. Molecular dynamics simulations showed that collagen complexes with 3 major ginger compounds exhibited lower root mean square deviations than collagen, maintained by hydrogen bonds and hydrophobic interactions. Given that 6-shogaol is a dehydration product of 6-gingerol (6-GOL), 6-GOL and gingerenone A (GGA) were selected for experimental validation. Ultraviolet-visible absorption and fluorescence spectroscopy showed 6-GOL and GGA interacted with collagen. Fourier transform infrared spectroscopy revealed that both compounds altered the Amide bands, confirming strengthened hydrogen bonding. Furthermore, differential scanning calorimetry analysis demonstrated that both compounds enhanced the thermal stability of collagen. These findings demonstrate that 6-GOL and GGA stabilize bovine type I collagen, providing insights into their potential as collagen stabilizers.