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Amyloid-β peptide dimers undergo a random coil to β-sheet transition in the aqueous phase but not at the neuronal membrane. | LitMetric

AI Article Synopsis

  • * Researchers performed molecular dynamics simulations to study the behavior of amyloid-β (Aβ)42 dimers in both water and a model of neuronal membranes.
  • * The study found that while Aβ42 dimers can become more ordered and toxic in solution, interactions with gangliosides (like GM1) on the membrane prevent this order and may protect against Aβ toxicity.

Article Abstract

Mounting evidence suggests that the neuronal cell membrane is the main site of oligomer-mediated neuronal toxicity of amyloid-β peptides in Alzheimer's disease. To gain a detailed understanding of the mutual interference of amyloid-β oligomers and the neuronal membrane, we carried out microseconds of all-atom molecular dynamics (MD) simulations on the dimerization of amyloid-β (Aβ)42 in the aqueous phase and in the presence of a lipid bilayer mimicking the in vivo composition of neuronal membranes. The dimerization in solution is characterized by a random coil to β-sheet transition that seems on pathway to amyloid aggregation, while the interactions with the neuronal membrane decrease the order of the Aβ42 dimer by attenuating its propensity to form a β-sheet structure. The main lipid interaction partners of Aβ42 are the surface-exposed sugar groups of the gangliosides GM1. As the neurotoxic activity of amyloid oligomers increases with oligomer order, these results suggest that GM1 is neuroprotective against Aβ-mediated toxicity.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8488611PMC
http://dx.doi.org/10.1073/pnas.2106210118DOI Listing

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