The role of α-Synuclein misfolding in Parkinson s disease

Vajiheh Eskandari¹

1) Department of Biology, University of Zanjan, Zanjan, 45371-38791, Iran

Publication : The 7th Iranian Conference on Bioinformatics (icb7.ir)
Abstract :
Parkinson disease (PD) is a progressive neurodegenerative disorder in the central nervous system. Misfolding and aggregation of alpha-synoclain is one of the important factors in the incidence and progression of Parkinson s disease [1]. α-Synuclein is a 140-amino acid protein which has been proposed that it may act like a prion: pathological forms of the protein may be capable of changing the conformation of normal alpha-synuclein to aggregation form [2]. In this study, the protein domains were obtained from of Alzheimer s beta-amyloid proteins, human and sheep prion and also alpha-synuclein Parkinson s protein. We then obtained the motifs from domains, and after review, the motifs of human and sheep prion and Alzheimer s beta amyloid, which had the smallest and most similarity to the alpha-synuclin protein motifs, were selected. The interactions of these motifs with Parkinson s Protein were investigated using Autodokc vina. Molecular dynamics simulating of docked molecules detect change in behavior of alpha-synuclein protein, which it may be attribute to changes in conformation of alpha-synuclein.
Keywords : α-Synuclein Parkinson Autodock