Fig. 2: Effect of various peptide primary structural features on activity.
From: The lexicon of antimicrobial peptides: a complete set of arginine and tryptophan sequences
a Activity (IC50) presented as a three-dimensional representation illustrating (as a landscape) the influence of the number of W and R residues on activity against the three different organisms. b Inhibitory activity plotted against percentage W residues within the sequence, faceted by peptide length (indicated at the top of each sub panel). The black spline through the data indicates the average activity for each peptide length. Error bars are within the markers and are ±s.e.m. (n = 4). Similar plots for MBC are shown in Supplementary Fig. 2a. c Analysis of average inhibitory and haemolytic activities for peptides with different numbers of isolated W singlets (W), duplets (WW) and triplets (WWW), faceted by peptide length (indicated at the top of each sub panel). Error bars shown are ±s.e.m. Similar plots for R, RR and RRR are shown in Supplementary Fig. 2bd Effect of percentage W content on average ODvis, faceted by peptide length (indicated at the top of each sub panel). Error bars shown are ±s.e.m. (n = 4). e Haemolytic activity plotted against percentage W residues within the sequence, faceted by peptide length (indicated at the top of each sub panel). The black spline through the data indicates the average activity for each peptide length. Error bars are within the markers and are ±s.e.m (n = 4). f Roughness analysis, indicating the extent of variability of activity across the three different antimicrobial activity landscapes. Error bars shown are ±s.e.m. (n = 100 in all cases).
