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Tesi etd-11202015-181900


Thesis type
Tesi di laurea magistrale
Author
ROVERE, MATTEO
URN
etd-11202015-181900
Title
Investigation of the folding and oligomerization equilibria of the amyloidogenic protein alpha-synuclein.
Struttura
CHIMICA E CHIMICA INDUSTRIALE
Corso di studi
CHIMICA
Supervisors
relatore Prof. Bartels, Tim
correlatore Prof. Di Bari, Lorenzo
controrelatore Prof.ssa Tinè, Maria Rosaria
Parole chiave
  • protein folding
  • neurodegeneration
  • protein misfolding
  • Parkinson's disease
  • protein oligomers
  • oligomerization
  • biophysics
  • swag
Data inizio appello
16/12/2015;
Consultabilità
Parziale
Data di rilascio
16/12/2018
Riassunto analitico
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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