Friedreich's ataxia (FRDA) is an autosomal recessive disorder, caused by reduced levels of the protein frataxin. This protein is located in the mitochondria, where it functions in the biogenesis of iron-sulphur clusters (ISCs), which are important for the function of the mitochondrial respiratory chain complexes.

Although Parkinson's disease is a complex multifactorial disorder, one key causal factor remains the misfolding and aggregation of the protein α‐Syn. The major histopathological hallmarks of Parkinson's Disease (PD) include the loss of dopaminergic neurons in substantia nigra and the presence of Lewy bodies, which are intracellular inclusions of aggregated α‐Syn.

Polyunsaturated fatty acid (PUFA) peroxidation is initiated by hydrogen atom abstraction at bis-allylic sites and sets in motion a chain reaction that generates multiple toxic products associated with numerous disorders.

Oxidative stress is associated with numerous neurological disorders. Mitochondrial malfunction contributes to generation of reactive oxygen species (ROS) in proximity to mitochondrial membranes rich in polyunsaturated fatty acids (PUFAs).

Substitution of −CD2– at the reactive centers of linoleic and linolenic acids reduces the rate of abstraction of D by a tocopheryl radical by as much as 36-fold, compared to the abstraction of H from a corresponding −CH2– center.

Friedreich ataxia is an autosomal recessive, inherited neuro- and cardio-degenerative disorder characterized by progressive ataxia of all four limbs, dysarthria, areflexia, sensory loss, skeletal deformities, and hypertrophic cardiomyopathy. Most disease alleles have a trinucleotide repeat expansion in the first intron of the FXN gene, which decreases expression of the encoded protein frataxin.