Fig. 5
From: Designed α-sheet peptides suppress amyloid formation in Staphylococcus aureus biofilms
Aggregation of synthetic PSMα1 is inhibited by designed α-sheet peptides. a Synthetic PSMα1 peptide (30 μM, 0.34% DMSO, pH 5) was allowed to aggregate alone and in the presence of AP90 (1:4 molar ratio) and RC (1:4 molar ratio). Two different solvent conditions were used (0.34% DMSO in water, blue bars; LB medium + 0.34% DMSO, red bars) and aggregation was monitored by ThT fluorescence. Inhibition values for each peptide are reported as a percentage of the peptide-free control samples (0% inhibition). Error bars represent the standard error of the mean of 3–6 replicates. b ThT fluorescence curves monitoring the aggregation kinetics of PSMα1 under the two different solvent conditions in panel a (water = blue curve; LB medium = red curve). c The contribution of individual LB medium components (10 g/L peptone, 5 g/L yeast extract, and 85 mM NaCl) to PSMα1 aggregation kinetics was also investigated. Fluorescence values in NaCl solution were quite high, so its curve is shown as an inset. All solutions contain 0.34% DMSO for consistency and solubilization of PSMα1. Values in b and c are averages of 3 samples, corrected by relevant PSMα1-free controls, with error bars to represent the standard deviation of the mean and curves are corrected by subtracting blanks lacking PSMα1
