2024
DOI: 10.1038/s41467-023-43821-y
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The structure of tyrosine-10 favors ionic conductance of Alzheimer’s disease-associated full-length amyloid-β channels

Abhijith G. Karkisaval,
Rowan Hassan,
Andrew Nguyen
et al.

Abstract: Amyloid β (Aβ) ion channels destabilize cellular ionic homeostasis, which contributes to neurotoxicity in Alzheimer’s disease. The relative roles of various Aβ isoforms are poorly understood. We use bilayer electrophysiology, AFM imaging, circular dichroism, FTIR and fluorescence spectroscopy to characterize channel activities of four most prevalent Aβ peptides, Aβ1-42, Aβ1-40, and their pyroglutamylated forms (AβpE3-42, AβpE3-40) and correlate them with the peptides’ structural features. Solvent-induced fluor… Show more

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Cited by 6 publications
(1 citation statement)
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“…Many of these studies have indicated pore formation in the membrane by both Aβ42 and Aβ40 oligomers. ,,, Molecular modeling has yielded β-sheet rich pore-forming oligomers (PFOs) of Aβ in the membrane. Stabilizing uniform Aβ oligomers with chemical protocols, , and subsequent probing with NMR , or XRD , have provided some of the first experimental 3D structures of Aβ oligomers. However, the physiological relevance of these stabilized oligomers is unknown.…”
mentioning
confidence: 99%
“…Many of these studies have indicated pore formation in the membrane by both Aβ42 and Aβ40 oligomers. ,,, Molecular modeling has yielded β-sheet rich pore-forming oligomers (PFOs) of Aβ in the membrane. Stabilizing uniform Aβ oligomers with chemical protocols, , and subsequent probing with NMR , or XRD , have provided some of the first experimental 3D structures of Aβ oligomers. However, the physiological relevance of these stabilized oligomers is unknown.…”
mentioning
confidence: 99%