Abstract
Numerous theoretical studies have been conducted on the effects of high-voltage electric fields on proteins, but few have produced experimental evidence. To acquire experimental data for the amyloid disassemble theory, we exposed transthyretin aggregates to 1 ns 1.26 MV/cm pulsed electric fields (PEFs) to promote transthyretin degradation. The process produced no changes in pH, and the resulting temperature increases were < 1 °C. We conclude that the physical effects of PEFs, rather than thermal or chemical effects, facilitate aggregate degradation.
Highlights
Numerous theoretical studies have been conducted on the effects of high-voltage electric fields on proteins, but few have produced experimental evidence
Much discussion has focused on membrane dynamics and damage, attention is shifting to proteins because membranes and their associated proteins, such as channels, pumps, actin cables, and microtubules, respond to electric fields, both theoretically and e xperimentally[7,8,9,10,11,12]
To examine direct electrical effects, purified proteins must be exposed to pulsed electric fields (PEFs), but membrane and membrane-associated proteins may be under a field of ≥ 1 MV/cm
Summary
Numerous theoretical studies have been conducted on the effects of high-voltage electric fields on proteins, but few have produced experimental evidence. Because it is technically challenging to apply strong electric fields to liquid samples, most previous studies have used numerical calculations[17,18,19,20,21]. According to these calculations, proteins change their three-dimensional structures under a static electric field of 1 MV/cm. Pandey et al presented results to support the theory, but they applied a weaker electric field of 230 kV/cm for longer than 40 h. Chemical, and physical effects of PEFs by applying 1,000 pulses at 1 ns, 1.26 MV/ cm to transthyretin aggregates
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