4.7 Article

Protein-Mediated Electroporation in a Cardiac Voltage-Sensing Domain Due to an nsPEF Stimulus

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MDPI
DOI: 10.3390/ijms241411397

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nsPEF; NPS; pores; complex pores; ionic channels; VSD; electroporation

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This study integrates molecular dynamics simulations and machine learning techniques to explore the physiological implications of nanosecond pulsed electric field (nsPEF). It uncovers a new and underexplored phenomenon, protein-mediated electroporation. By focusing on the voltage-sensing domain (VSD) of the NaV1.5 sodium cardiac channel, the researchers analyze the structures that form pores under nsPEF stimulation, providing insights into the defibrillation effect of nsPEF. The findings reveal that the selected VSD of NaV1.5 forms pores in a distinct manner from traditional VSD opening, expanding our understanding of nsPEF and its interaction with protein channels.
This study takes a step in understanding the physiological implications of the nanosecond pulsed electric field (nsPEF) by integrating molecular dynamics simulations and machine learning techniques. nsPEF, a state-of-the-art technology, uses high-voltage electric field pulses with a nanosecond duration to modulate cellular activity. This investigation reveals a relatively new and underexplored phenomenon: protein-mediated electroporation. Our research focused on the voltage-sensing domain (VSD) of the NaV1.5 sodium cardiac channel in response to nsPEF stimulation. We scrutinized the VSD structures that form pores and thereby contribute to the physical chemistry that governs the defibrillation effect of nsPEF. To do so, we conducted a comprehensive analysis involving the clustering of 142 replicas simulated for 50 ns under nsPEF stimuli. We subsequently pinpointed the representative structures of each cluster and computed the free energy between them. We find that the selected VSD of NaV1.5 forms pores under nsPEF stimulation, but in a way that significant differs from the traditional VSD opening. This study not only extends our understanding of nsPEF and its interaction with protein channels but also adds a new effect to further study.

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