Apolipoprotein A-I binding to anionic vesicles and lipopolysaccharides: Role for lysine residues in antimicrobial properties

► apoA-I binding to LPS was strongly reduced upon acetylation of lysine residues. ► apoA-I shows a much stronger binding interaction with PG compared to PC. ► Acetylated protein lost most of the PG binding activity. ► Antimicrobial activity was reduced for acetylated apoA-I. ► Electrostatic forces are critical for binding of apoA-I to LPS and PG.