Antimicrobial peptides (AMPs) are small, typically cationic peptides that exhibit strong antibacterial properties. The target of most AMPs has been shown to be the bacterial cell membrane.  We present a summary of computational and theoretical investigations of protegrin, a particularly potent AMP.We have carried out extensive molecular dynamics simulations to investigate the structure and dynamics of protegrin pores in membrane-mimicking lipid bilayers.  We have extracted pore structures from these simulations and used them as input to an approximate continuum transport model (the Poisson-Nernst-Planck equations) in order to capture nonequilibrium, steady-state ion transport through the pore in the presence of an applied voltage. We have used the computed ion permeabilities as inputs to a model of transient ion transport between an entire cell and its surrounding medium.    Overall, our work provides a quantitative mechanistic description of the mechanism of action of protegrin antimicrobial peptides across multiple length and time scales.

Multiscale models of antimicrobial peptides

244th National Meeting (2012)

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