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Identification and quantification of adducts between oxidized rosmarinic acid and thiol compounds by UHPLC-LTQ-Orbitrap and MALDI-TOF/TOF tandem mass spectrometry.

LTQ Orbitrap MS/MS was used to identify the adducts between quinones derived from rosmarinic acid (RosA) and thiol compounds, including cysteine (Cys), glutathione (GSH), and peptides digested from myosin. Two adducts of quinone-RosA/Cys and quinone-RosA/2Cys, one quinone-RosA/GSH adduct, and three quinone-RosA/peptide adducts were identified by extracted ion and MS(2) fragment ion chromatograms. By using MALDI-TOF/TOF MS, the adduction reaction between RosA and myosin in myofibrillar protein isolates was determined, demonstrating that the accurate reaction site was at Cys949 of myosin. The effect of reaction conditions, including stirring time, temperature, and oxidative stress, on the formation of adducts was further investigated. The formation of quinone-RosA/Cys and quinone-RosA/GSH increased with stirring time. Both adducts increased with temperature, whereas the reactivity of the addition reaction of GSH was higher than that of Cys. With increasing oxidation stress, the formation of quinone-RosA/GSH adduct increased and that of quinone-RosA/Cys adduct decreased.