Interfacial Effects on the Conformation of Amyloid-Beta Peptide

Seidler, Norbert W.; Eklund, Joshua D.

doi:10.2174/092986609787316324

Cited by 2 publications

(2 citation statements)

References 24 publications

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“…If, in fact, the higher potency of HFIP-prepared versus NaOH-prepared Aβ oligomers that we report is associated with HFIP effects on the aggregation process, the aggregation pathway of endogenous Aβ in the brain might also be affected by other fluorinated substances. Indeed, the interactions between Aβ and fluorinated inhalational anesthetics are well documented [73], [74], [75], [76]. HFIP is structurally related to sevoflurane and is a sevoflurane metabolite while TFA is an isoflurane metabolite.…”

Section: Discussionmentioning

confidence: 99%

Effect of Synthetic Aβ Peptide Oligomers and Fluorinated Solvents on Kv1.3 Channel Properties and Membrane Conductance

et al. 2012

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The impact of synthetic amyloid β (1–42) (Aβ1–42) 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 Aβ1–42 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 Aβ1–42 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, Aβ1–42 solutions had no effect on Kv 1.3 channel properties. Aβ1–42 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 Aβ1–42 peptide), and trifluoroacetic acid (TFA) (used during Aβ1–42 synthesis), we determined concentrations of these fluorinated compounds in the stock Aβ1–42 solutions by 19F NMR. After extensive evaporation, the concentration of HFIP in the 100× stock Aβ1–42 solutions was ∼1.7 μM. The concentration of residual TFA in the 70× stock Aβ1–42 solutions was ∼20 μM. Even at the stock concentrations neither HFIP nor TFA alone had any effect on potassium currents or BLMs. The Aβ1–42 oligomers prepared with HFIP as solvent, however, were more potent in the electrophysiological tests, suggesting that fluorinated compounds, such as HFIP or structurally-related inhalational anesthetics, may affect Aβ1–42 aggregation and potentially enhance ability of oligomers to modulate voltage-gated ion channels and biological membrane properties.

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Section: Discussionmentioning

confidence: 99%

Effect of Synthetic Aβ Peptide Oligomers and Fluorinated Solvents on Kv1.3 Channel Properties and Membrane Conductance

et al. 2012

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“…Several amyloid-forming peptides and proteins are surface-active [24][25][26][27][28][29]. Interaction of amyloid-forming proteins and peptides with membranes [30][31][32][33][34][35][36] and lipid monolayers [37][38][39] has been investigated.…”

Section: Introductionmentioning

confidence: 99%

Self-assembly of short amyloidogenic peptides at the air–water interface

Chaudhary¹,

Nagaraj²

2011

Journal of Colloid and Interface Science

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Interfacial Effects on the Conformation of Amyloid-Beta Peptide

Cited by 2 publications

References 24 publications

Effect of Synthetic Aβ Peptide Oligomers and Fluorinated Solvents on Kv1.3 Channel Properties and Membrane Conductance

Effect of Synthetic Aβ Peptide Oligomers and Fluorinated Solvents on Kv1.3 Channel Properties and Membrane Conductance

Self-assembly of short amyloidogenic peptides at the air–water interface

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