Isolevuglandin adduct (IsoLG adduct (occasionally abbreviated as IsoLG-protein adduct))

Isolevuglandin adduct formation refers to the covalent attachment of highly reactive lipid-derived dicarbonyl compounds called isolevuglandins (IsoLGs) to primary amine groups on proteins, most notably lysine residues. This process occurs rapidly under conditions of oxidative stress when polyunsaturated fatty acids are peroxidized by enzymes such as cyclooxygenase or via free radical mechanisms. The resulting IsoLG–protein adducts can cause irreversible protein modifications that disrupt normal function—including cross-linking and aggregation—and generate neoantigens that activate immune responses. These modified proteins have been implicated in a wide range of diseases associated with oxidative injury and inflammation, including hypertension, atrial fibrillation, heart failure, Alzheimer’s disease, cancer, atherosclerosis, renal dysfunction, mitochondrial disorders, and more. In some contexts—for example in antigen-presenting cells during high-salt intake—IsoLG-adducted proteins act as neoantigens that drive autoimmune-like inflammation contributing to organ damage such as kidney injury or cardiac dysfunction. While not themselves therapeutic targets in the traditional sense (i.e., not receptors or enzymes), strategies aimed at scavenging IsoLGs before they form damaging protein adducts are being explored therapeutically.[1][3][5]

Other names

Isolevuglandin-protein adductIsoLG–protein adductIsolevuglandin-modified protein

Scavenging of reactive isolevuglandins to prevent covalent protein modification and subsequent immune activation or tissue injury[1].