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A causative agent of Alzheimer's disease (AD) is a short amphipathic peptide called amyloid beta (Aβ). Aβ monomers undergo structural changes leading to their oligomerization or fibrillization. The monomers as well as all aggregated forms of Aβ, i.e., oligomers, and fibrils, can bind to biological membranes, thereby modulating membrane mechanical properties. It is also known that some isoforms of the large-conductance calcium-activated potassium (BK_Ca) channel, including the mitochondrial BK_Ca (mitoBK_Ca) channel, respond to mechanical changes in the membrane. Here, using the patch-clamp technique, we investigated the impact of full-length Aβ (Aβ_1–42) and its fragment, Aβ_25–35, on the activity of mitoBK_Ca channels. We found that all forms of Aβ inhibited the activity of the mitoBK_Ca channel in a concentration-dependent manner. Since monomers, oligomers, and fibrils of Aβ exhibit different molecular …