Figure 2

Peptide structure and lipid complex formation activity of RG33. (a) Circular dichroism spectroscopy of RG33 dissolved in PBS at 0.2 mg/ml. This spectrum represents the average of five measurements using five separate solutions. (b) Helical wheel analysis of residues 209 to 241 of the ApoA-I protein. One-letter code for amino acids is used and numbered 1 to 33 with start at residue 209. (c) rHDL particles were prepared by incubating the MLVs with RG33 peptide in the molar ratios noted at 24 °C for four days. Particle size distribution was analysed by DLS and frequency curves generated for RG33. Both MLVs alone (data on pure 100 nm MLVs is adapted from15) and lipid-free peptide are included as controls. GraphPad Prism (version 8.0) (www.graphpad.com) was used. Data represents five individual experiments.