Apolipoprotein D acts as a chaperone of Aβ peptide delaying its assembly into amyloid aggregates.

ABSTRACT: The accumulation of amyloid-β (Aβ) peptides is at the root of Alzheimer's disease (AD), where oligomeric forms of Aβ disrupt brain physiology before any sign of dementia. Intense research has been directed to extrinsic molecules that modulate Aβ aggregation. However, more knowledge is needed about endogenous mechanisms maintaining Aβ homeostasis in a healthy brain. The Lipocalin Apolipoprotein D (ApoD) displays neuroprotective functions, many of which rely on managing lipids in cell membranes or lipoprotein particles. ApoD is upregulated in the aging brain and AD and is present in amyloid-β plaques. However, the functional relationship of ApoD with Aβ peptides aggregation needs to be studied. Using aggregation and ligand binding assays guided by molecular dynamics modeling, in this work we

SUBMITTER: Mondejar-Duran J 

PROVIDER: S-EPMC13635072 | biostudies-literature | 2026 Jul

REPOSITORIES: biostudies-literature