Back to Search
Start Over
Decreased Water Mobility Contributes To Increased α-Synuclein Aggregation.
- Source :
-
Angewandte Chemie (International ed. in English) [Angew Chem Int Ed Engl] 2023 Feb 06; Vol. 62 (7), pp. e202212063. Date of Electronic Publication: 2023 Jan 12. - Publication Year :
- 2023
-
Abstract
- The solvation shell is essential for the folding and function of proteins, but how it contributes to protein misfolding and aggregation has still to be elucidated. We show that the mobility of solvation shell H <subscript>2</subscript> O molecules influences the aggregation rate of the amyloid protein α-synuclein (αSyn), a protein associated with Parkinson's disease. When the mobility of H <subscript>2</subscript> O within the solvation shell is reduced by the presence of NaCl, αSyn aggregation rate increases. Conversely, in the presence CsI the mobility of the solvation shell is increased and αSyn aggregation is reduced. Changing the solvent from H <subscript>2</subscript> O to D <subscript>2</subscript> O leads to increased aggregation rates, indicating a solvent driven effect. We show the increased aggregation rate is not directly due to a change in the structural conformations of αSyn, it is also influenced by a reduction in both the H <subscript>2</subscript> O mobility and αSyn mobility. We propose that reduced mobility of αSyn contributes to increased aggregation by promoting intermolecular interactions.<br /> (© 2022 The Authors. Angewandte Chemie International Edition published by Wiley-VCH GmbH.)
- Subjects :
- Humans
Water
Solvents
alpha-Synuclein chemistry
Parkinson Disease
Subjects
Details
- Language :
- English
- ISSN :
- 1521-3773
- Volume :
- 62
- Issue :
- 7
- Database :
- MEDLINE
- Journal :
- Angewandte Chemie (International ed. in English)
- Publication Type :
- Academic Journal
- Accession number :
- 36316279
- Full Text :
- https://doi.org/10.1002/anie.202212063