Format

Send to

Choose Destination
See comment in PubMed Commons below
Biophys J. 2013 Aug 20;105(4):899-910. doi: 10.1016/j.bpj.2013.06.046.

Embedding Aβ42 in heterogeneous membranes depends on cholesterol asymmetries.

Author information

1
Department of Physics, University of Roma Tre, Roma, Italy.

Abstract

Using a coarse-grained lipid and peptide model, we show that the free energy stabilization of amyloid-β in heterogeneous lipid membranes is predicted to have a dependence on asymmetric distributions of cholesterol compositions across the membrane leaflets. We find that a highly asymmetric cholesterol distribution that is depleted on the exofacial leaflet but enhanced on the cytofacial leaflet of the model lipid membrane thermodynamically favors membrane retention of a fully embedded Aβ peptide. However, in the case of cholesterol redistribution that increases concentration of cholesterol on the exofacial layer, typical of aging or Alzheimer's disease, the free energy favors peptide extrusion of the highly reactive N-terminus into the extracellular space that may be vulnerable to aggregation, oligomerization, or deleterious oxidative reactivity.

PMID:
23972842
PMCID:
PMC3752101
DOI:
10.1016/j.bpj.2013.06.046
[Indexed for MEDLINE]
Free PMC Article
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Elsevier Science Icon for PubMed Central
    Loading ...
    Support Center