Figure 3
From: Development of novel broad-spectrum antimicrobial lipopeptides derived from plantaricin NC8 β
Hemolytic activity of full length and modified peptides of PLNC8 β. The hemolytic activity was determined on human erythrocytes (15% suspended in PBS) after (A) exposure to the peptides with different lengths of FA chains using the indicated concentrations for 1 h. Hemolytic activity was associated with the length of the FA chain, where conjugation of long FA chain (≥ 7 carbon atoms) rendered the peptides to be more hemolytic. Hemolytic activity of the L-enantiomers (B) and D-enantiomer (C) of 6-C(5–7) of both isoleucine and leucine variants. Replacement of all three isoleucine residues with leucine rendered the lipopeptide to be more hemolytic. (D) Hemolytic activity at 100 µM in regard to FA chain length.
