The role of α-Synuclein misfolding in Parkinson s disease
محل انتشار: هفتمین همایش بیوانفورماتیک ایران
سال انتشار: 1396
نوع سند: مقاله کنفرانسی
زبان: انگلیسی
مشاهده: 393
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شناسه ملی سند علمی:
IBIS07_078
تاریخ نمایه سازی: 29 فروردین 1397
چکیده مقاله:
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.
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نویسندگان
Vajiheh Eskandari
Department of Biology, University of Zanjan, Zanjan, ۴۵۳۷۱-۳۸۷۹۱, Iran