Quantification of pulsed electric field for the rupture of giant vesicles with various surface charges, cholesterols and osmotic pressures

Electropermeabilization is a promising phenomenon that occurs when pulsed electric field with high frequency is applied to cells/vesicles. We quantify the required values of pulsed electric fields for the rupture of cell-sized giant unilamellar vesicles (GUVs) which are prepared under various surface charges, cholesterol contents and osmotic pressures. The probability of rupture and the average time of rupture are evaluated under these conditions. The electric field changes from 500 to 410 Vcm-1 by varying the anionic lipid mole fraction from 0 to 0.60 for getting the maximum probability of rupture (i.e., 1.0). In contrast, the same probability of rupture is obtained for changing the electric field from 410 to 630 Vcm-1 by varying the cholesterol mole fraction in the membranes from 0 to 0.40. These results suggest that the required electric field for the rupture decreases with the increase of surface charge density but increases with the increase of cholesterol. We also quantify the electric field for the rupture of GUVs containing anionic mole fraction of 0.40 under various osmotic pressures. In the absence of osmotic pressure, the electric field for the rupture is obtained 430 Vcm-1, whereas the field is 300 Vcm-1 in the presence of 17 mOsmL-1, indicating the instability of GUVs at higher osmotic pressures. These investigations open an avenue of possibilities for finding the electric field dependent rupture of cell-like vesicles along with the insight of biophysical and biochemical processes.

The Effects of Pulsed Electric Field On The Interaction Between SARS-Cov-2 And Human ACE2: Y505 Is A Key Target

A novel coronavirus has rapidly spread to almost every country in the world, causing over 233 million confirmed cases of coronavirus disease 2019 (COVID-19) and over 209,761,242 deaths by late September 2021. Binding the receptor binding domain (RBD) to the host cell surface receptor protein, angiotensin converter enzyme (ACE2), is a key step in virus infection. In this study, we applied a pulsed electric field to the RBD/ACE2 complex based on molecular dynamics simulation and demonstrated that the electric field affects the structure and binding affinity of the complex. Additionally, residue Y505 is the crucial medium for the effects of electric field on the complex. Overall, these results may help apply an external electric field to virus suppression.