Tesi etd-11202015-181900 |
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Tipo di tesi
Tesi di laurea magistrale
Autore
ROVERE, MATTEO
URN
etd-11202015-181900
Titolo
Investigation of the folding and oligomerization equilibria of the amyloidogenic protein alpha-synuclein.
Dipartimento
CHIMICA E CHIMICA INDUSTRIALE
Corso di studi
CHIMICA
Relatori
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
Parole chiave
- biophysics
- neurodegeneration
- oligomerization
- Parkinson's disease
- protein folding
- protein misfolding
- protein oligomers
- swag
Data inizio appello
16/12/2015
Consultabilità
Completa
Riassunto
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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