The hemolytic activity of Latarcin-2a Wt and mutant peptides were determined using fresh bovine blood. The solution containing 1% isolated RBCs were exposed to varying concentrations of LTC-2a W and Mt peptides. After 24 h of incubation, the amount of hemoglobin released upon lysis of RBCs was determined by measuring the absorbance at 414 nm.
Figure 2: Hemolytic activity of Ltc-2a Wt and Ltc-2a Mt. The hemolytic activity of Ltc-2a Wt and Ltc-2a Mt was determined by subjecting the RBCs isolated from bovine blood to various concentration of peptides. The plot represents the amount of hemoglobin released upon lysis estimated by measuring absorbance at 414nm.
It was observed that Ltc-2a Wt showed hemolytic activity up to 16 µM concentration, whereas Ltc-2a Mt did not show any hemolytic activity. Our data reveal that the presence of F10K mutation in Ltc-2a Mt suppresses the hemolytic activity of the antimicrobial peptide when compared to the wild type.