Antimicrobial · Aromatic-rich, C-terminally amidated antimicrobial peptide
Temporin L
Also known as TL
An aromatic-rich temporin used to investigate lipid disruption, lipopolysaccharide interactions and membrane selectivity.
- Length
- 13 amino acids
- Half-life
- Not well characterised
- Mechanism
- Temporin L associates with lipid membranes and lipopolysaccharide, adopting membrane-associated conformations that promote bilayer disruption. Its principal activity is not assigned to a defined protein receptor, and interactions with other temporins can modify peptide aggregation in lipopolysaccharide-containing models.
- Studied in
- Bacterial cultures, lipid vesicles, lipopolysaccharide-binding assays and erythrocyte membrane assays investigate membrane selectivity and cooperative peptide behaviour.
About Temporin L
Temporin L is a 13-residue peptide from the skin secretions of Rana temporaria, within the temporin family first described in 1996. Its mature sequence is FVQWFSKFLGRIL-NH₂. Unlike Temporin B, it contains several aromatic residues, including one tryptophan and three phenylalanines, together with lysine and arginine. The peptide is C-terminally amidated and contains no cysteine. These sequence features support investigations of how aromatic side chains and positive charge contribute to membrane association.
Experimental work examines Temporin L in both bacterial and non-bacterial membrane systems because strong membrane interactions need not be selective for a single membrane type. Its tryptophan provides an intrinsic fluorescence probe for changes in the local molecular environment. Lipopolysaccharide-containing models are also used to investigate its interactions with other temporins, particularly Temporin B. Cooperative behaviour in these systems is interpreted through peptide binding, aggregation and membrane disruption rather than a defined protein receptor.
Laboratory notes
- For research use only; include non-bacterial membrane controls when assessing selectivity rather than relying solely on bacterial growth assays.
- For intrinsic tryptophan fluorescence measurements, control for scattering, inner-filter effects and fluorescence from other assay components.
- Check solubility and aggregation under the actual assay conditions, and keep solvent content matched across samples and controls.
Storage and reconstitution basics: storage guide.
Questions about Temporin L
What distinguishes Temporin L from Temporin B?
Both contain 13 residues and a C-terminal amide, but Temporin L has more aromatic residues and includes both lysine and arginine, producing different membrane-interaction properties.
Why is fluorescence useful for studying Temporin L?
Its single tryptophan can report changes in local polarity through fluorescence shifts, supporting studies of membrane association when appropriate optical controls are included.
Do bacterial assays alone establish membrane selectivity?
No. Parallel assays using different lipid compositions or non-bacterial membrane models are needed to distinguish bacterial activity from more general membrane disruption.
Is Temporin L for human use?
No. It is supplied strictly for in-vitro laboratory research and is not for human or animal consumption.
Related research peptides
All products are sold for laboratory research use only. Not for human consumption, not a medicine, not for diagnosing, treating or preventing any condition.