Resolving pulsed electric field effects on proteins in bulk aqueous solution
Externally applied macroscopic electric fields can couple to protein charge distributions and potentially alter protein conformation and function. Whether they produce persistent changes in bulk aqueous protein solutions remains unresolved because electrode-based field delivery can also cause electrochemical reactions whose extent depends on the exposure regime. Here we test this distinction…
The study investigates the impact of pulsed electric fields (PEF) on protein conformation and function in a bulk aqueous solution. The researchers focus on tubulin, a key component of microtubules, which serves as a functional readout for the effects of PEF. Intense PEF treatment resulted in a tubulin gel-like zone near the anode of the electrode and a persistent decrease in the microtubule assembly's ability to polymerise.
Additionally, a minor alteration in the tubulin subpopulation was observed. Colourimetric pH mapping and physicochemical modelling revealed a zone of decreased pH at the anode, spatially corresponding to the gel-like tubulin zone. By modifying pulse protocols to suppress local pH changes without reducing overall electrical exposure, the researchers found that structural and functional perturbations were no longer detectable in tubulin.
These findings, supported by energetic estimates, demonstrate that persistent responses observed for tubulin are due to electrochemically generated pH changes and highlight significant constraints on large persistent effects arising from direct field-protein coupling in bulk aqueous systems.
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