Post-translational modifications (PTMs) afford proteins new functions to reshape their interactomes and orchestrate complex cellular responses to environmental cues or signaling molecules. Oxidative PTMs of proteins by lipid-electrophiles have been implicated in pathogenesis of tumors through modulation of signaling pathways controlling cell growth, division and apoptosis1-3. However, conventional genetic/biochemical means, such as si/shRNA knockdown and site-directed mutagenesis, are not suited to study protein-PTM interactions in a spatiotemporally controlled manner. Therefore, we developed a genome-wide chemoproteomic platform to enable precision tracking of lipid-electrophile PTMs in living systems1, 4-5. This platform engendered the discovery of an isozyme-specific cysteine hydroxynonenylation occurring on Akt3 oncogenic kinase, which ultimately initiates apoptosis in cells. In this talk, I will focus on the development of Akt3 isozyme-specific covalent inhibitors through hijacking this innate oxidative PTM. The pharmacological advantages of such compounds in vivo will be compared to conventional pan-Akt kinase inhibitors in clinical trials. Our findings further promise a novel gateway to the design and development of isozyme-specific covalent ligands derived from understanding precise oxidative PTMs at the molecular level.