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For research use only — not for human consumption
Fowlicidin-1 original Regena research vial

Antimicrobial · Avian cathelicidin antimicrobial peptide

Fowlicidin-1

Also known as Gallinacin-3

Fowlicidin-1 is a 26-amino-acid chicken cathelicidin studied for its ability to disrupt bacterial membranes and neutralize lipopolysaccharide (LPS).

Length
26 amino acids
Half-life
Not well characterised
Mechanism
It disrupts bacterial membranes through pore formation and can also bind to bacterial lipopolysaccharide (LPS), neutralizing its endotoxic effects.
Studied in
Laboratory investigations examine its bactericidal activity, particularly against Gram-negative bacteria, and its capacity to neutralize endotoxins in vitro.

About Fowlicidin-1

Fowlicidin-1 is a cathelicidin-family antimicrobial peptide found in chickens (Gallus gallus). The mature peptide consists of 26 amino acids and is processed from a larger pro-peptide precursor. As a component of the avian innate immune system, it provides a model for studying host defense peptides in non-mammalian vertebrates.

The peptide exhibits a potent and rapid bactericidal effect, primarily by forming pores in microbial membranes. A key area of its research is its strong affinity for lipopolysaccharide (LPS), the major component of the outer membrane of Gram-negative bacteria. This binding can both facilitate membrane disruption and neutralize the endotoxic activity of LPS in various in vitro assay systems.

Laboratory notes

  • Fowlicidin-1 is highly cationic and may adhere to negatively charged surfaces like standard glass or plastic; use low-protein-binding tubes.
  • For LPS neutralization assays, pre-incubation of the peptide with LPS is a common experimental step.
  • Store lyophilized powder at -20°C and reconstituted solutions in small aliquots at -80°C to avoid freeze-thaw cycles.

Storage and reconstitution basics: storage guide.

Questions about Fowlicidin-1

What is a cathelicidin?

Cathelicidins are a family of antimicrobial peptides found in vertebrates, characterized by a conserved N-terminal 'cathelin' domain and a variable C-terminal antimicrobial peptide domain, like Fowlicidin-1.

Is Fowlicidin-1 more active against certain types of bacteria?

In vitro studies frequently report high activity against Gram-negative bacteria, which is attributed to its strong interaction with LPS.

How does its structure relate to its function?

It forms an amphipathic α-helix in membrane-mimicking environments, which allows it to insert into and destabilize the lipid bilayer of bacterial cells.

Is Fowlicidin-1 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.