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- W2061893670 abstract "Oxidatively damaged lipid membranes are known to promote the aggregation of amyloid β (Aβ) proteins and fibril formation. When lipid membranes contain ω-6 polyunsaturated fatty acyl chains, 4-hydroxy-2-nonenal (HNE) is produced during oxidative stress. We previously demonstrated that HNE modifies the three His residues in Aβ proteins by Michael addition, which increases the hydrophobicity and affinity of Aβ proteins for the membrane surface, and promotes the aggregation of unmodified Aβ proteins into fibrils. There are two different mechanisms by which the promotion of fibril formation may occur. HNE-modified Aβ proteins may act as catalytic templates that stabilize monomers in a fibrillar conformation, but do not ultimately become a part of the fibril (template mechanism). Alternatively, they may act as seeds that reduce a kinetic barrier to adopt a fibrillar conformation by becoming a part of the fibril (seed mechanism). In this report, the concentrations of HNE-modified Aβ proteins in fibrils, in solution, and in lipid vesicle membranes were monitored in order to distinguish between these two mechanisms.Results indicate that HNE-modified Aβ proteins associate primarily with lipid membranes, suggesting that HNE promotes fibril formation by the template mechanism, and that relatively little HNE-modified Aβ is incorporated into fibrils. This result is pathophysiologically significant because such templates are not consumed by the process of fibril formation and may be long-lived. The formation of isolated templates may also account for the patchy distribution of amyloid fibril plaques in brain tissue afflicted with Alzheimer's disease." @default.
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- W2061893670 date "2009-02-01" @default.
- W2061893670 modified "2023-09-26" @default.
- W2061893670 title "Amyloid β Proteins, Modified by a Lipid Oxidation Product, Are Nucleation Sites for Fibril Formation on Lipid Membranes" @default.
- W2061893670 doi "https://doi.org/10.1016/j.bpj.2008.12.310" @default.
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