Fig. 2: Secondary structure analysis of pleurocidin peptides. | Communications Biology

Fig. 2: Secondary structure analysis of pleurocidin peptides.

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

Fig. 2: Secondary structure analysis of pleurocidin peptides.

Top view snapshots showing ordered/disordered conformation for each of eight peptide monomers (a, d, g) binding to POPE/POPG bilayers in silico. From the same simulations, average psi dihedral angles and circular variance of psi are shown for each residue, averaged over 200 ns of simulation and eight peptides (b, e, h). Far-UV CD spectra obtained in anionic SDS detergent micelles or models of Gram-negative or Gram-positive plasma membranes comprising, respectively, POPE/POPG or POPG lipids (c, f, i). Data are shown for pleurocidin (a–c), pleurocidin-KR (d–f) and pleurocidin-VA (g–i).

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