Abstract
In presence of chemical, mechanical or electromagnetic stimuli, protein functions and characteristics can highly differ from physiological conditions. In this work we investigate, at atomistic details, the way in which high intensity electric field pulses can be transduced into biophysical effects mainly related to protein unfolding by comparing the effect of three different waveforms of the pulses on protein behavior. Results from molecular dynamics simulations of a globular protein, namely myoglobin, have shown that real Gaussian and Bipolar pulses with lower energy but higher spectral frequency content can induce effects similar to an ideal rectangular pulse. Index Terms-Pulsed electric fields, molecular dynamics, protein unfolding.
Highlights
Pulsed electric fields of high intensity and different durations are at the basis of electroporation, an extremely promising technology developing since 90’s, with important applications in the fields of: biomedical science [1,2,3]; biotechnology with useful implications in food preserving [4]; nanotechnology with outcomes for bio-sensing [5] and protein analysis for binding characterization [6].It is well known that intense electric fields can profoundly affect the physical properties and reactivity of dissolved molecules
The investigation of protein-unfolding effects induced by different waveforms of high intensity electric field pulses becomes extremely interesting
The simulated system consisted of a 6-nm side rectangular box, where a single myoglobin and 6740 Single Point Charge (SPC) [24] water molecules resulting in a typical density of 1000 kg/m3
Summary
Pulsed electric fields of high intensity and different durations are at the basis of electroporation, an extremely promising technology developing since 90’s, with important applications in the fields of: biomedical science [1,2,3]; biotechnology with useful implications in food preserving [4]; nanotechnology with outcomes for bio-sensing [5] and protein analysis for binding characterization [6].It is well known that intense electric fields can profoundly affect the physical properties and reactivity of dissolved molecules. One of the best acknowledged physical mechanisms at the basis of ms- and μs-pulsed electric fields is a significant increase of cell membrane permeability due to pores creation [9], when the pulse duration goes down to the nanosecond scale, and signal intensities reach tens of MV/m, different mechanisms can be postulated: in particular a possible effect on protein denaturation and folding [10]. Given this framework, the investigation of protein-unfolding effects induced by different waveforms of high intensity electric field pulses becomes extremely interesting. A rigorous study of protein-induced effects would be useful for a real comprehension of the mechanisms underlying possible protein denaturation
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
