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Open AccessArticle

In Silico Study of the Mechanism of Binding of the N-Terminal Region of α Synuclein to Synaptic-Like Membranes

1
Department of Life Sciences, Imperial College London, South Kensington, London SW7 2AX, UK
2
Department of Pharmacy, University of Naples “Federico II”, 80131 Naples, Italy
*
Author to whom correspondence should be addressed.
Life 2020, 10(6), 98; https://doi.org/10.3390/life10060098
Received: 15 May 2020 / Revised: 17 June 2020 / Accepted: 22 June 2020 / Published: 26 June 2020
The membrane binding by α-synuclein (αS), a presynaptic protein whose aggregation is strongly linked with Parkinson’s disease, influences its biological behavior under functional and pathological conditions. This interaction requires a conformational transition from a disordered-unbound to a partially helical membrane-bound state of the protein. In the present study, we used enhanced coarse-grained MD simulations to characterize the sequence and conformational determinants of the binding to synaptic-like vesicles by the N-terminal region of αS. This region is the membrane anchor and is of crucial importance for the properties of the physiological monomeric state of αS as well as for its aberrant aggregates. These results identify the key factors that play a role in the binding of αS with synaptic lipid bilayers in both membrane-tethered and membrane-locked conformational states. View Full-Text
Keywords: α-Synuclein; membrane binding; disorder-to-order transition; coarse-grained simulations; Parkinson’s disease α-Synuclein; membrane binding; disorder-to-order transition; coarse-grained simulations; Parkinson’s disease
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Navarro-Paya, C.; Sanz-Hernandez, M.; De Simone, A. In Silico Study of the Mechanism of Binding of the N-Terminal Region of α Synuclein to Synaptic-Like Membranes. Life 2020, 10, 98.

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