Designed α-sheet peptides suppress amyloid formation in Staphylococcus aureus biofilms

Screening of designed peptides for inhibition of amyloid formation in S. aureus biofilms. a Schematic of protocol for testing designed α-sheet peptides in S. aureus biofilm cultures with an illustration of the main-chain structure of the AP90 α-sheet design. b A panel of designed α-sheet peptides (AP90, AP401, and AP407), as well as random coil (RC) and β-hairpin controls (β), was tested against two S. aureus strains, MN8 (hashed bars) and SH1000 WT (white bars). ThT fluorescence fluorescence values indicate the extent of amyloid formation in the EM and are shown as the percent of peptide-free control conditions. c Dose-response curve for the designed peptide AP90 against S. aureus MN8 biofilms reveals a significant decrease in EM amyloid content as the concentration of AP90 is increased. Error bars in b and c represent the standard error of the mean for experiments performed in triplicat