Multispectral and molecular dynamics study on the impact of trans, trans-2,4-decadienal and 4-hydroxy-2-nonenal on myoglobin redox stability

[Display omitted] •The effects of tt-DDE and HNE on the structural changes in myoglobin were explored.•The pro-oxidant effect of tt-DDE on myoglobin is stronger than that of HNE.•tt-DDE is more prone to combine with myoglobin to form complexes than HNE.•The interaction types and sites of tt-DDE and HNE to myoglobin were illustrated. This study investigated the interaction between myoglobin (Mb) and two lipid oxidation products, 4-hydroxy-2-nonenal (HNE) and trans, trans-2,4-decadienal (tt-DDE), at pH 5.6 and 7.4 through the combination of multispectral and molecular dynamics simulations. In this study, tt-DDE was more prone to promote Mb oxidation than HNE by loosening the Mb structure, which is associated with more destroyed secondary and tertiary structures. Furthermore, the pro-oxidation of both lipid products was stronger at pH 5.6 than at pH 7.4. The molecular docking revealed that both tt-DDE and HNE were combined closely with the heme group of Mb. And tt-DDE had hydrogen bonds, hydrophobic interactions, and van der Waals forces with Mb, but HNE only had hydrophobic interactions. In conclusion, it was firstly found that tt-DDE was also shown to have high activity in promoting Mb oxidation as another important aldehyde from lipid oxidation products.