Abstract
Human apolipoprotein E (apoE), which plays a central role in lipid and cholesterol metabolism, exists in three major isoforms: E2, E3, and E4. The E4 allele is a major genetic factor for late-onset Alzheimer's disease (AD), while the E2 allele is thought to be protective. ApoE was shown to be connected to the aggregation, degradation, and clearance of toxic soluble oligomers of disordered amyloid-beta (Aβ) peptides, which are central to AD pathogenesis. However, previously reported interactions between apoE and Aβ are ambiguous since they rarely account for the dynamic and transient nature of Aβ oligomers or the aggregation and lipidation of apoE.
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