Alarin but not its alternative-splicing form, GALP (Galanin-like peptide) has antimicrobial activity.
Wada. Akihiro A; Wong. Pooi-Fong PF; Hojo. Hironobu H; Hasegawa. Makoto M; Ichinose. Akitoyo A; Llanes. Rafael R; Kubo. Yoshinao Y; Senba. Masachika M; Ichinose. Yoshio Y
Key Findings
- Alarin inhibits growth of E. coli in a radial diffusion assay, similar in potency to LL‑37.
- The conserved N‑terminal region of alarin is required for its antimicrobial effect; truncating it reduces killing ability.
- Alarin causes bacterial membrane blebbing but does not cause hemolysis of human red blood cells, and it is ineffective against gram‑positive Staphylococcus aureus.
Practical Outcomes
- At this stage alarin is not a ready‑to‑use supplement; the data are early‑stage lab results. However, the finding suggests that peptides like alarin could be explored for gut‑health or infection‑prevention strategies that avoid damaging blood cells. Enthusiasts should watch for future research before considering any self‑experimentation.
Summary
Researchers found that alarin, a brain peptide, can kill the gut bacterium E. coli in lab tests, working about as well as the well‑known antimicrobial peptide LL‑37. It does this without breaking red blood cells, but it only works on gram‑negative bugs like E. coli and not on gram‑positive ones such as Staph.
Abstract
Alarin is an alternative-splicing form of GALP (galanin-like peptide). It shares only 5 conserved amino acids at the N-terminal region with GALP which is involved in a diverse range of normal brain functions. This study seeks to investigate whether alarin has additional functions due to its differences from GALP. Here, we have shown using a radial diffusion assay that alarin but not GALP inhibited the growth of Escherichia coli (strain ML-35). The conserved N-terminal region, however, remained essential for the antimicrobial activity of alarin as truncated peptides showed reduced killing effect. Moreover, alarin inhibited the growth of E. coli in a similar potency as human cathelicidin LL-37, a well-studied antimicrobial peptide. Electron microscopy further showed that alarin induced bacterial membrane blebbing but unlike LL-37, it did not cause hemolysis of erythrocytes. In addition, alarin is only active against the gram-negative bacteria, E. coli but not the gram-positive bacteria, Staphylococcus aureus. Thus, these data suggest that alarin has potentials as an antimicrobial and should be considered for the development in human therapeutics.
Study Information
pubmed
2013
2013-03-26T00:00:00.000Z
10.1016/j.bbrc.2013.03.045
20
30