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FEBS Lett. 2019 Jun;593(11):1144-1153. doi: 10.1002/1873-3468.13428. Epub 2019 May 27.

Apolipoprotein E associated with reconstituted high-density lipoprotein-like particles is protected from aggregation.

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Nanobiophysics Group, Technical Medical Centre, Faculty of Science and Technology, University of Twente, Enschede, The Netherlands.
Structural Biology Brussels, Department of Biotechnology (DBIT), Vrije Universiteit Brussel (VUB), Belgium.
Structural Biology Research Center, VIB, Brussels, Belgium.
Department of Neurology, Washington University School of Medicine, St. Louis, MO, USA.
Applied Stem Cell Technologies, Faculty of Science and Technology, University of Twente, Enschede, The Netherlands.


Apolipoprotein E (APOE) genotype determines Alzheimer's disease (AD) susceptibility, with the APOE ε4 allele being an established risk factor for late-onset AD. The ApoE lipidation status has been reported to impact amyloid-beta (Aβ) peptide metabolism. The details of how lipidation affects ApoE behavior remain to be elucidated. In this study, we prepared lipid-free and lipid-bound ApoE particles, mimicking the high-density lipoprotein particles found in vivo, for all three isoforms (ApoE2, ApoE3, and ApoE4) and biophysically characterized them. We find that lipid-free ApoE in solution has the tendency to aggregate in vitro in an isoform-dependent manner under near-physiological conditions and that aggregation is impeded by lipidation of ApoE.


Alzheimer's disease; aggregation; apolipoprotein E; high-density lipoprotein; isoform; lipidation

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