Two byproducts of reactive oxidative species (ROS) and subsequent lipid peroxidation, 4-hydroxy-2-nonenal (4HNE) and 4-oxo-nonenal (4ONE), can adduct to proteins and cause cytotoxicity in cells. Through incubation and tryptic digestion, the goal of this study was to understand the adduction patterns of 4HNE and 4ONE with electron transfer protein (ETF) along with several other model peptides. ETF is at risk of alteration by 4HNE and 4ONE which can prevent ETF from properly acting as a conduit of electrons from fatty acid oxidation to the electron transport chain. In this study, methods were developed for LC-MS analyses of tryptic peptides of ETF. The results suggest that 4HNE is more likely to adduct to lysine residues of ETF through Michael addition than to the histidine or cysteine residues of ETF. For incubations that included the reductant sodium borohydride, no Schiff base adductions to lysine residues were observed.

Mass spectrometric analyses of 4 hydroxy-nonenal and 4 oxo-nonenal adducts to electron transfer flavoprotein

ACS Spring 2022

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