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Amyloid pores are membrane-spanning structures formed by the oligomerization of amyloidogenic peptides, primarily amyloid-β (Aβ). These pores disrupt cellular ion homeostasis, particularly calcium, and are implicated in neurotoxicity in Alzheimer's disease. They are typically composed of small Aβ oligomers assembled into β-barrel-like structures that insert into lipid bilayers, acting as non-selective cation channels. Targeting these pores represents a therapeutic strategy for AD.
Inhibition of amyloid pore formation; Stabilization of amyloid-beta monomers/oligomers to prevent pore formation; Blockage of ion channel activity of amyloid pores
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