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Plasticity of Membrane Binding by the Central Region of α-Synuclein. | LitMetric

AI Article Synopsis

  • Interaction with membranes causes αS to gain some helical structure while still remaining partly disordered, which is crucial for its function in clumping synaptic vesicles.
  • Researchers used advanced simulations to examine how different structures of αS affect its ability to bind to membranes, shedding light on its role in both normal cellular functions and disease-related aggregation and toxicity.

Article Abstract

Membrane binding by α-synuclein (αS), an intrinsically disordered protein whose aggregation is associated with Parkinson's disease, is a key step in determining its biological properties under both physiological and pathological conditions. Upon membrane interaction, αS retains a partial level of structural disorder despite acquiring α-helical content. In the membrane-bound state, the equilibrium between the helical-bound and disordered-detached states of the central region of αS (residues 65-97) has been involved in a double-anchor mechanism that promotes the clustering of synaptic vesicles. Herein, we investigated the underlying molecular bases of this equilibrium using enhanced coarse-grained molecular dynamics simulations. The results enabled clarifying the conformational dependencies of the membrane affinity by this protein region that, in addition to playing a role in physiological membrane binding, has key relevance for the aggregation of αS and the mechanisms of the toxicity of the resulting assemblies.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9240306PMC
http://dx.doi.org/10.3389/fmolb.2022.857217DOI Listing

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