iProXProteomicsChunhui ZhangBos Taurushttp://www.iprox.org/page/project.html?id=IPX0017375000dr_zch@163.comChinese Academy of Agricultural SciencesiProXThis investigation aimed to clarify the binding mechanisms between six aldehydes and myofibrillar proteins (MPs), with a structural explanation in response to stage-heating treatments. The conformational intermediates of MPs, which form during heat processing, were systematically characterized to elucidate their role in aldehyde binding and flavor retention. Machine learning results suggested that high-temperature boiling promoted extensive protein denaturation and aggregation, while subsequent low-temperature stewing induced partial rearrangement. Thermodynamic parameters indicated that hexanal-MPs formation was primarily driven by hydrogen bonding, whereas other longer-chain and unsaturated aldehydes penetrated hydrophobic pockets. Proteomics revealed that saturated aldehydes predominantly formed Schiff bases with the lysine ε-amino group. Unsaturated aldehydes, especially (E, E)-2,4-decadienal, undergo both Schiff base reactions and Michael addition with cysteine, histidine, and tryptophan residues. The retention/release behavior of aldehydes during processing is determined by covalent and non-covalent interactions. These results provide a scientific basis for precisely controlling flavor quality in meat products.Novel insights into the binding mechanisms of selected aldehydes during heat-induced protein unfolding.Wang Jingfan J, Wang Tianze T, Yang Ping P, Han Dong D, Zhang Chunhui C, Jia Wei W, Purcaro Giorgia G, Fauconnier Marie-Laure MLfalseNovel insights into the binding mechanisms of selected aldehydes during heat-induced protein unfoldingThe heated aldehyde-MPs solution was washed twice with NH₄HCO₃ (200 µL of 50 mM) buffer solution and then centrifuged (12,000 rpm, 5 min). Samples were alkylated with 5 μL of iodoacetamide for 1 h, subsequently undergoing tryptic digestion at 37 °C for 16 h (enzyme-to-protein ratio 1:50, w/w). The digestion was quenched with 2 μL of 1% formic acid, and the peptides were analyzed by LC-MS/MS. The MS/MS spectra were then searched against the UniProt database using Proteome Discoverer 2.4.Fri May 29 00:00:00 BST 2026PXD079095991342215494