Temporins

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.^[3]

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.^[4]