Molecular mechanisms of myofibrillar protein-aldehydes interactions: Carbon chain length-dependent binding site...

In this study, the potential mechanism of the interaction between aldehydes and myofibrillar protein (MP) was systematically examined using various analytical techniques. The findings showed that the binding affinity of MP toward aldehydes was positively correlated with their carbon chain length, indicating that molecular structure play a role in their interaction. Multispectral analysis revealed that the incorporation of aldehydes induced spatial conformational changes in MP and reduced structural order. Additionally, atomic force microscopy demonstrated that aldehydes and MP locally aggregated to form complexes through non-covalent interactions. Further investigations involving thermodynamic analysis, validation of key chemical bonds, and molecular docking experiments elucidated the effects of carbon chain length and non-covalent interactions on binding strength. It was confirmed that hydrophobic interactions predominantly governed these non-covalent interactions, with a stronger influence observed as carbon chain length increased. This study provided valuable insights for controlling flavor profiles of meat products.