Description
Temporin L is a hydrophobic peptide amide derived from the frog Rana temporaria. This peptide penetrates the hydrophobic core of the cell membrane to penetrate and disrupt the lipid bilayer. Temporin L enhances Temporin A and Temporin B activity by preventing their oligomerization to Lipopolysaccharide (LPS), allowing them to bypass LPS and access the cytoplasmic membrane. This peptide is active against Gram-positive and Gram-negative bacteria, including B. megaterium and E. coli