Effect of familial parkinson's disease point mutations A30P and A53T on the structural properties, aggregation, and fibrillation of human alpha-synuclein

Two point mutations, A53T and A30P, in the alpha-synuclein gene lead to self-association of the molecule as opposed to the wild-type. Data indicate that self-association in the mutants is due to an increased propensity for aggregation of the partially folded intermediates, which eventually leads to fibrillation of alpha-synuclein.