Fig. 3: Activity of pleurocidin and its analogues on in silico and in vitro models of bacterial plasma membranes. | Communications Biology

Fig. 3: Activity of pleurocidin and its analogues on in silico and in vitro models of bacterial plasma membranes.

From: A pleurocidin analogue with greater conformational flexibility, enhanced antimicrobial potency and in vivo therapeutic efficacy

Fig. 3: Activity of pleurocidin and its analogues on in silico and in vitro models of bacterial plasma membranes.

The depth of insertion into each membrane is shown as the Z-position for each residue, averaged over all four peptides, relative to the phosphate group plane in the upper POPE/POPG (a, e, i) or POPG (c, g, k) bilayer leaflet in six MD simulations. Positive or negative values indicate the peptides are below or above the phosphate group. Representative current traces illustrating membrane activity when DPhPE/DPhPG (b, f, j) or DPhPG (d, h, l) model membranes are challenged with each peptide at the lowest concentration that induced detectable activity. Data are for pleurocidin (a–d), pleurocidin-KR (e–h) and pleurocidin-VA (i–l). Membrane disordering by each peptide in mixed POPE/POPG bilayers is shown with data obtained from 2H solid-state NMR (m, n) or from MD simulations where order parameters are calculated for all lipids within 4 Å of a peptide (o, p).

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