Temporins are a family of

peptide Peptides are short chains of amino acids linked by peptide bonds. A polypeptide is a longer, continuous, unbranched peptide chain. Polypeptides that have a molecular mass of 10,000 Da or more are called proteins. Chains of fewer than twenty am ...

s isolated originally from the skin secretion of the European red frog, ''

Rana temporaria The common frog or grass frog (''Rana temporaria''), also known as the European common frog, European common brown frog, European grass frog, European Holarctic true frog, European pond frog or European brown frog or simply the frog, is a semi- ...

''. Peptides belonging to the temporin family have been isolated also from closely related North American frogs, such as ''Rana sphenocephala''.

Discovery

In 1996, the skin of the ''Rana temporaria'' was screened into a cDNA library, discovering three peptide precursors, known as Temporin B, Temporin G, and Temporin H. Once discovered, the three peptide, along with other temporins found in the sample, were separated from secretions of the frog's skin. Biological assays were performed, revealing that all temporins, in exception of temporin D and H, exhibited antibacterial activity. It was soon discovered that other species of frog also possess temporal, resulting in the discovery of more than 150 peptides from the temporin family. Some of the genera of frogs include the ''Amolops, Hylarana, Lithobathes, Odorrana, Pelophylax, Rana, and Hylarana.''

Clinical uses

Temporins are a family of antimicrobial peptides (AMPs), which are highly targetable toward Gram-positive bacteria, allowing it to penetrate the cell wall and damage the inner membrane of the bacteria. These proteins are also capable of killing specific cancer cells when they are locally administered to a tumor, making it a good anticancer drug.

References

{{Reflist Peptides