Malondialdehyde, a lipoperoxidation-derived aldehyde, can bring about secondary oxidative damage to proteins.

Lipoperoxidation-derived aldehydes, for example malondialdehyde (MDA), can damage proteins by generating covalent adducts whose accumulation probably participates in tissue damage during aging. However, the mechanisms of adduct formation and their stability are scarcely known. This article investigates whether oxidative steps are involved in the process. As a model of the process, the interaction between MDA and bovine serum albumin (BSA) was analyzed. Incubation of BSA with MDA resulted in rapid quenching of tryptophan fluorescence and appearance of MDA protein adduct fluorescence; transition metal ion traces interfered with the latter process. MDA induced generation of peroxides in BSA, which was preventable with the antioxidant 2,6,-di-tert-butyl-4-methylphenol (BHT). MDA-exposed BSA underwent aggregation, degradation, and BHT-sensitive "gel retardation" effects. Phycoerythrin fluorescence disappearance, a marker of damage mediated by reactive oxygen species, indicated synergism between MDA and metal ions. The interaction between reactive aldehydes and proteins is likely to occur in several steps, some of them oxidative in nature, giving rise to advanced lipoperoxidation end-products, which could participate, with advanced glycation end-products, in the generation of tissue damage during aging.