Oxidative stress refers to the physiological stress caused by an imbalance between the systemic production of reactive oxygen species and the biological system’s ability to detoxify the reactive intermediates. It is a condition where the system lacks its ability to repair the damage due to oxidative stress and thus leading to a number of diseases. Usually, the impact of oxidative stress on a cell is measured by analysing the oxidation states of molecules like glutathione. Similarly, the stress induced perturbations can be overviewed by analysing the post-translational modifications associated with different protein components. Carbonylation of proteins, one of the major oxidative stress induced modifications, can be considered as potential biomarkers for measuring the level of oxidative stresses. Recent investigations has revealed that carbonylation of proteins occur primarily at amino acid residues, proline, arginine, lysine, threonine etc. As part of the on-going studies, we aim at characterizing the carbonylated proteins from various model systems undergoing oxidative stresses. The brief workflow includes isolation and enrichment of carbonylated proteins by biotin-avidin affinity chromatography followed by their identification and quantitation by mass spectrometry (MS). We also aim at testing the efficacy of various natural products as potential anti-oxidants through MS based proteomics strategies
