PORTO @ 
Archivio Istituzionale della Ricerca
IRIS è la soluzione IT che facilita la raccolta e la gestione dei dati relativi alle attività e ai prodotti della ricerca. Fornisce a ricercatori, amministratori e valutatori gli strumenti per monitorare i risultati della ricerca, aumentarne la visibilità e allocare in modo efficace le risorse disponibili.
EnglishAlzheimer 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.
Highlighting the effect of amyloid beta assemblies on the mechanical properties and conformational stability of cell membrane / Grasso, G.; Lionello, C.; Stojceski, F.. - In: JOURNAL OF MOLECULAR GRAPHICS & MODELLING. - ISSN 1093-3263. - 100(2020), p. 107670.
| Titolo: | Highlighting the effect of amyloid beta assemblies on the mechanical properties and conformational stability of cell membrane | |
| Autori: | ||
| Data di pubblicazione: | 2020 | |
| Rivista: | ||
| Digital Object Identifier (DOI): | http://dx.doi.org/10.1016/j.jmgm.2020.107670 | |
| Appare nelle tipologie: | 1.1 Articolo in rivista |
File in questo prodotto:
| File | Descrizione | Tipologia | Licenza | |
|---|---|---|---|---|
| 1-s2.0-S1093326320304599-main.pdf | 2a Post-print versione editoriale / Version of Record | Non Pubblico - Accesso privato/ristretto | Administrator Richiedi una copia | |
| 1-s2.0-S1093326320304599-mmc1.pdf | Appendix A. Supplementary data | Altro materiale allegato | Non Pubblico - Accesso privato/ristretto | Administrator Richiedi una copia |
| Manuscript.pdf | 2. Post-print / Author's Accepted Manuscript |  | Embargo: 06/07/2022 Richiedi una copia |
http://hdl.handle.net/11583/2845968
Copyright © 2021