AI Article Synopsis
- Human α-synuclein (αSyn) is an intrinsically disordered protein involved in neurotransmitter trafficking, but its roles in brain cells are not fully understood.
- The protein can aggregate into amyloid forms linked to diseases, and this self-assembly is influenced by its interactions with lipid membranes, particularly in low-water environments.
- The review focuses on the molecular dynamics of αSyn's interactions with lipid membranes and water, examining how these factors contribute to its self-assembly and potential pathological functions.
Article Abstract
Human α‑synuclein (αSyn) is an intrinsically disordered protein (IDP) whose biological and pathological functions in brain neuronal cells have not yet been fully elucidated. αSyn intrinsically participates in aiding neurotransmitter trafficking through αSyn the association with lipid membranes. However, lipid-associated states of αSyn also induce amyloid self-assembly that is linked to the pathogenesis of various synucleinopathies. These contradicting actions arise from the limited water content near lipid-water interfaces that controls αSyn electrostatic and hydrophobic interactions. Thus, understanding the molecular interactions between αSyn and lipid membranes in the presence of water molecules is critical in elucidating the pivotal role of lipid-associated αSyn in amyloid self-assembly. In this review, we describe how the membrane interface controls electrostatic and hydrophobic interactions of lipid-associated αSyn. Moreover, membrane amyloid self-assembly of αSyn will be further discussed with regards to the structural dynamics of lipid-associated αSyn and water molecules near the interface.
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| http://dx.doi.org/10.1016/j.bbamem.2018.02.007 | DOI Listing |
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