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Highlighting the effect of amyloid beta assemblies on the mechanical properties and conformational stability of cell membrane.
Journal article

Highlighting the effect of amyloid beta assemblies on the mechanical properties and conformational stability of cell membrane.

  • Grasso G Istituto Dalle Molle di studi sull'Intelligenza Artificiale (IDSIA), Scuola Universitaria Professionale della Svizzera italiana (SUPSI), Università della Svizzera italiana (USI), Centro Galleria 2, Manno, CH-6928, Switzerland. Electronic address: gianvito.grasso@idsia.ch.
  • Lionello C Department of Applied Science and Technology, Politecnico di Torino, Corso Duca degli Abruzzi 24, 10129, Torino, Italy.
  • Stojceski F Istituto Dalle Molle di studi sull'Intelligenza Artificiale (IDSIA), Scuola Universitaria Professionale della Svizzera italiana (SUPSI), Università della Svizzera italiana (USI), Centro Galleria 2, Manno, CH-6928, Switzerland.
  • 2020-07-26
Published in:
  • Journal of molecular graphics & modelling. - 2020
Alzheimer disease
Amyloid beta
Amyloid oligomer
Amyloid peptide
Area per lipid
Aβ
Bending modulus
Computational modelling
Membrane destabilization
Membrane fibril interaction
Membrane thickness
Molecular dynamics
Order parameter
gromacs
English Alzheimer disease (AD) is the most common cause of dementia, characterized by a progressive decline in cognitive function due to the abnormal aggregation and deposition of Amyloid beta (Aβ) fibrils in the brain of patients. In this context, the molecular mechanisms of protein misfolding and aggregation that are known to induce significant biophysical alterations in cells, including destabilization of plasma membranes, remain partially unclear. Physical interaction between the Aβ assemblies and the membrane leads to the disruption of the cell membrane in multiple ways including, surface carpeting, generation of transmembrane channels and detergent-like membrane dissolution. Understanding the impact of amyloidogenic protein in different stages of aggregation with the plasma membrane, plays a crucial role to fully elucidate the pathological mechanisms of AD. Within this framework, computer simulations represent a powerful tool able to shed lights on the interactions governing the structural influence of Aβ proteins on biological membrane. In this study, molecular dynamics (MD) simulations have been performed in order to characterize how POPC bilayer conformational and mechanical properties are affected by the interaction with Aβ11-42 peptide, oligomer and fibril.
Language
  • English
Open access status
closed
Identifiers
Persistent URL
https://folia.unifr.ch/global/documents/188934
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