Understanding the dynamics of monomeric, dimeric, and tetrameric α-synuclein structures in water.
FEBS Open Bio
; 6(7): 666-86, 2016 07.
Article
em En
| MEDLINE
| ID: mdl-27398307
Human α-synuclein (αS) is an intrinsically disordered protein associated with Parkinson's disease. Molecular mechanisms of corruptive misfolding and aggregation of αS resulting in the disease, as well as the structure and other properties of the corresponding oligomers are not entirely understood yet, preventing the development of efficient therapies. In this study, we investigate the folding dynamics of initially unfolded hypothetical αS constructs in water using all-atom molecular dynamics simulations. We also employ the novel essential collective dynamics method to analyze the results obtained from the simulations. Our comparative analysis of monomeric, dimeric, and tetrameric αS models reveals pronounced differences in their structure and stability, emphasizing the importance of small oligomers, particularly dimers, in the process of misfolding.
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01-internacional
Base de dados:
MEDLINE
Idioma:
En
Revista:
FEBS Open Bio
Ano de publicação:
2016
Tipo de documento:
Article