Extended Data Fig. 7: Characterization of PbgA-derived, synthetic LAB peptides.
From: Structure of the essential inner membrane lipopolysaccharide–PbgA complex
a, Biotinylated LAB peptides were captured and interferometry measurements measured upon presenting peptides to different concentrations of detergent solubilized lipids (LPS, phosphatidylethanolamine, phosphatidylglycerol and cardiolipin). Three independent experiments were performed and data shown are representative. b, CFUs of E. coli ATCC 25922 measured over time with LABv2.1 and polymyxin B. Data are mean ± s.d. for n = 3 independent cultures. c, A red blood cell (RBC) lysis assay evaluated after 18 h in the presence of indicated compounds (Methods). Data are mean ± s.d. (n = 3) for each compound tested. d, A RBC lysis assay comparing LABv2.1 precursors (LABWT, LABWT+, LABv2.0) and LABv2.1 analogues designed, based on the LPS–PbgA crystal structure, to disrupt specific interactions of lipid A (LABv2.1_Dap213Thr, LABv2.1_Dap213Arg, LABv2.1_Dap212-Met213). Data are mean ± s.d. for n = 3 independent assay of each compound at each concentration.
