Temporin L Amide Antimicrobial Peptide

Temporin L is a 13-residue C-terminally amidated antimicrobial peptide from the European red frog Rana temporaria. It is a hydrophobic, amphipathic peptide that associates with lipid bilayers and can disrupt bacterial membranes. Published studies also show that Temporin L can enhance the activity of other temporins against Gram-negative bacteria by reducing peptide oligomerization within the lipopolysaccharide barrier.

• antimicrobial peptide assays
• membrane-interaction studies
• liposome and lipid-bilayer research
• temporin synergy studies

Temporin L is hydrophobic and can adsorb to surfaces or show limited aqueous solubility at higher concentrations. Solvent, ionic strength and lipid composition should be controlled when comparing membrane activity.

1. A Synergism between Temporins toward Gram-negative Bacteria Overcomes Resistance Imposed by the Lipopolysaccharide Protective Layer
2. Binding of the Antimicrobial Peptide Temporin L to Liposomes Assessed by Trp Fluorescence
3. Temporins, Antimicrobial Peptides from the European Red Frog Rana temporaria