Molecular Dynamics Simulations of the effect of Trifluoroethanol on the Conformation of a-synuclein peptide
کد مقاله : 1262-PHYSCHEM20
آتنا پاکزادیان *، سیف اله جلیلی
چکیده مقاله:
The accumulation of alpha-synuclein (α-syn) fibrils in neuronal inclusions is the defining pathological process in Parkinsondisease (PD). Solvation structure and association alpha-synuclein (α-syn) in aqueous TFE solutions are investigated.
Using molecular dynamics simulation and the AMBER03 force field. This conformational transition with concomitant peptide aggregation is a possible mechanism of plaque formation. Here, in order to gain more insight into the mechanism of α-helix formation of α-syn peptide by TFE, which particularly stabilizes α- helical conformation, we studied the secondary-structural elements of α-syn peptide by molecular dynamics simulations. Secondary structural elements determined from NMR spectroscopy in aqueous TFE solution are preserved during the MD simulation. TFE/water mixed solvent has reduced capacity for forming hydrogen bond to the peptide compared to pure water solvent. TFE allows α-syn to form bifurcated hydrogen bonds to TFE as well as to residues in peptide itself. MD simulation in this study supports the notion that TFE can act as a α-helical structure forming solvent.
کلیدواژه ها:
Alpha-synuclein (α-syn); Parkinson disease (PD); Hydrogen bond; TFE; MD simulatio
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