Effect of synthetic aβ peptide oligomers and fluorinated solvents on Kv1.3 channel properties and membrane conductance.

PloS One
Maria I LioudynoJames E Hall

Abstract

The impact of synthetic amyloid β (1-42) (Aβ(1-42)) oligomers on biophysical properties of voltage-gated potassium channels Kv 1.3 and lipid bilayer membranes (BLMs) was quantified for protocols using hexafluoroisopropanol (HFIP) or sodium hydroxide (NaOH) as solvents prior to initiating the oligomer formation. Regardless of the solvent used Aβ(1-42) samples contained oligomers that reacted with the conformation-specific antibodies A11 and OC and had similar size distributions as determined by dynamic light scattering. Patch-clamp recordings of the potassium currents showed that synthetic Aβ(1-42) oligomers accelerate the activation and inactivation kinetics of Kv 1.3 current with no significant effect on current amplitude. In contrast to oligomeric samples, freshly prepared, presumably monomeric, Aβ(1-42) solutions had no effect on Kv 1.3 channel properties. Aβ(1-42) oligomers had no effect on the steady-state current (at -80 mV) recorded from Kv 1.3-expressing cells but increased the conductance of artificial BLMs in a dose-dependent fashion. Formation of amyloid channels, however, was not observed due to conditions of the experiments. To exclude the effects of HFIP (used to dissolve lyophilized Aβ(1-42) peptide), and trifluo...Continue Reading

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Citations

Sep 1, 2015·ACS Chemical Neuroscience·Ravit MalishevRaz Jelinek
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Jun 16, 2015·Frontiers in Neuroscience·Donghui ZhuSholpan Askarova
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Apr 4, 2021·Journal of Clinical Medicine·Alexandru CojocaruEugen Osiac

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Methods Mentioned

BETA
NMR
dynamic light scattering
Dot blots
dot-blot

Software Mentioned

OriginLab
XwinNMR
OriginPro7
OriginPro

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