A coarse grain model for alpha-synuclein aggregation in "High Performance Computing on CRESCO infrastructure: research activities and results 2014"

α-Synuclein (α-syn), a disordered cytoplasmatic protein involved in membrane trafficking in brain cells, plays a fundamental role in the pathogenesis of Parkinson’s disease (PD) and is one of the major components of the malignant fibrillar β-aggregates (Lewy bodies) found in the substantia nigra of PD suffering patients. It has been recently shown that the peptidyl prolyl isomerase FKBP12, especially abundant in the central nervous system, enhances aggregation of α-synuclein in vitro and in vivo. FKBP12 overexpression or unbalancing in brain cells has been hence proposed as a possible cause for neurological disorders. In this study, we devise a rudimental coarse grain model based on the hydrophobic/hydrophilic effect in order to simulate and rationalize the observed morphologies and kinetics in α-synuclein aggregation processes with or without FKBP12.