Parkinson's Disease (PD) is a neurological disorder increasingly affecting the aging population worldwide. The presence of Lewy bodies is the cause of PD, where fibrillar alpha-synuclein is the major component. This report describes the electrochemical analysis of alpha-synuclein protein in the presence of factors that accelerate or inhibit the rate of its aggregation. Baicalein is an electro-active flavonoid that can act as a metal-chelator and form several products including quinones upon oxidation. Exposure to Cu(II) ions is known to cause significant acceleration in the rate of alpha-synuclein fibril formation. Square-wave voltammetry (SWV) of alpha-synuclein in the presence of these electro-active factors revealed distinct interfacial changes attributed to complex formation of alpha-synuclein with these species in vitro. The role of baicalein as a fibrillogenesis inhibitor was found to be most effective during the early stages of the fibril formation. The proof-of-principal results indicate that electrochemistry as a drug screening technique can provide a powerful tool for the discovery of new fibrillogenesis inhibitors as promising therapeutics for neurodegenerative diseases. (C) 2010 Elsevier B.V. All rights reserved.