Fig. 6
From: Designed α-sheet peptides suppress amyloid formation in Staphylococcus aureus biofilms
Designed α-sheet peptides preferentially bind α-sheet-rich PSMα1 over fresh or fibrillar PSMα1. a Synthetic PSMα1 peptides (30 μM, 0.34% DMSO, pH 5) were allowed to aggregate as in Fig. 5, and matched samples were removed periodically from the plate for binding assessment using an agarose bead, resin-based assay and biolayer interferometry. Error bars represent the standard deviation of six samples. b In the resin-based assay, AP193-functionalized beads preferentially bound α-sheet rich PSMα1 (48 h) over earlier time points (0 and 24 h). Error bars represent the standard error of the mean over six samples. c In biolayer interferometry experiments, the equilibrium dissociation constant, KD, indicates preferential binding between AP90 and α-sheet-rich PSMα1 (~48 h) as opposed to α-helix-rich (~0 h) or β-sheet-rich states (~150 h). Note that 150 h is still in the sigmoidal region of the transition and some α-sheet is present
