Antimicrobial · Antimicrobial Peptide (AMP)
Gomesin
An 18-residue AMP from a spider with a beta-hairpin structure, studied for its broad antimicrobial and in-vitro cytotoxic effects on cancer cells.
- Length
- 18 amino acids
- Half-life
- Not well characterised
- Mechanism
- Gomesin disrupts microbial membranes via a beta-hairpin structure and also exhibits cell-penetrating properties in some experimental models.
- Studied in
- Laboratory studies investigate its broad-spectrum antimicrobial activity, its effects on cancer cell lines in-vitro, and the role of its disulfide-stabilised structure.
About Gomesin
Gomesin is an 18-amino-acid cationic antimicrobial peptide isolated from the hemocytes (blood cells) of the tarantula *Acanthoscurria gomesiana*. Its structure is characterised by a beta-hairpin fold stabilised by two disulfide bridges, a motif it shares with the tachyplesin family of peptides. This rigid, amphipathic structure is key to its biological activities.
In microbiology research, Gomesin is studied for its potent, broad-spectrum activity against Gram-positive and Gram-negative bacteria, fungi, and protozoa, mediated primarily through membrane disruption. Additionally, it has gained attention in cancer research for its ability to selectively induce apoptosis in various cancer cell lines in-vitro, while showing lower toxicity to non-cancerous cells in the same assays. The mechanisms behind this selectivity are an active area of investigation.
Laboratory notes
- The two disulfide bonds are essential for maintaining the beta-hairpin structure and biological activity; avoid harsh reducing conditions.
- When studying its effects on eukaryotic cells, use assays that can distinguish between necrosis and apoptosis (e.g., Annexin V/PI staining).
- Compare its in-vitro cytotoxicity against a panel of cancer cell lines and non-transformed control cell lines to characterise its selectivity index.
Storage and reconstitution basics: storage guide.
Questions about Gomesin
What is a beta-hairpin structure?
A beta-hairpin is a simple protein motif where two antiparallel beta-strands are connected by a short loop. In Gomesin, this structure is stabilised by two disulfide bridges.
From what animal was Gomesin first discovered?
It was originally isolated from the hemocytes, or blood cells, of the Brazilian spider *Acanthoscurria gomesiana*.
How does Gomesin's structure compare to Thanatin?
Both peptides feature a beta-hairpin structure stabilized by disulfide bonds. However, Gomesin has two disulfide bridges and 18 amino acids, while Thanatin has one disulfide bridge and 21 amino acids, leading to different overall shapes and target specificities.
Is Gomesin 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.