Speaker
Description
Pulsed electric fields (PEFs) are increasingly recognized for their ability to modulate protein structure and function, offering applications in biomedicine, food technology, and nanotechnology. Proteins, as electrically charged biomolecules, are highly responsive to PEFs, which can induce structural changes such as rotation, unfolding, and modifications to secondary structures. Molecular dynamics simulations and experimental studies have shown that intense PEFs in the megavolt per meter (MV/m) range realign protein dipoles, destabilize conformations, and expose hydrophobic residues, leading to aggregation. These effects have been observed in proteins like ubiquitin and ovalbumin through methods such as circular dichroism and fluorescence spectroscopy.
Beyond structural changes, PEFs influence functional properties, including enzymatic activity and protein self-assembly. Studies have demonstrated altered activity in enzymes like α-amylase and pectinase, as well as reversible and irreversible effects on tubulin and amyloid fibril assemblies. These findings highlight the potential of PEFs for targeted therapeutic interventions, enzyme regulation in food processing, and control over biomolecular assembly in nanotechnology.
Despite these advancements, further research is needed to explore the effects of PEFs on membrane proteins and refine the mechanistic understanding of protein-field interactions. The ability of PEFs to induce precise and non-thermal modifications makes them a promising tool for advancing science and technology across disciplines.
