Thesis etd-11202015-181900 |
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Thesis type
Tesi di laurea magistrale
URN
etd-11202015-181900
Thesis title
Investigation of the folding and oligomerization equilibria of the amyloidogenic protein alpha-synuclein.
Department
CHIMICA E CHIMICA INDUSTRIALE
Course of study
CHIMICA
Supervisors
.
relatore Prof. Bartels, Tim
correlatore Prof. Di Bari, Lorenzo
controrelatore Prof.ssa Tinè, Maria Rosaria
correlatore Prof. Di Bari, Lorenzo
controrelatore Prof.ssa Tinè, Maria Rosaria
Keywords
- biophysics
- neurodegeneration
- oligomerization
- Parkinson's disease
- protein folding
- protein misfolding
- protein oligomers
- swag
Graduation session start date
16/12/2015
Availability
Full
Abstract (Inglese)
Abstract (Italiano)
Alpha-synuclein is a protein involved in the pathogenesis of several neurodegenerative diseases and widely studied both for its remarkable biophysical properties and its clinical relevance. The affinity of alpha-synuclein for curved membranes and the fact that it acquires an alpha-helical structure when interacting with lipid bilayers have long been known. Recently, a tetrameric alpha-helical form of alpha-synuclein was isolated and characterized. We propose a connection between the membrane-binding equilibrium and the formation of the tetramer in a physiological environment. The aim of this project is to establish a refolding protocol for tetrameric alpha-synuclein and investigate the effects of brain-related cofactors on the lipid binding and oligomerization behaviour of the protein.
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