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

This study investigated the interaction between myoglobin (Mb) and two lipid oxidation products, 4-hydroxy-2nonenal (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.

Automated summary

This study investigated the interaction between myoglobin (Mb) and two lipid oxidation products, 4-hydroxy-2nonenal (HNE) and trans, trans-2,4-decadienal (tt-DDE), at different pH values. It was found that tt-DDE promoted the oxidation of Mb by destroying its structure, and this promotion was stronger at pH 5.6. Molecular docking results showed that both tt-DDE and HNE interacted with the heme group of Mb, but in different ways.