Osaka-university previously identified an antimicrobial peptide named AG30 (angiogenic peptide 30) that contained 30 amino acids and possessed both angiogenic and antibacterial functions. They designed a modified AG30 peptide (AG30/5C) by replacing several of the amino acid to improve angiogenic and antibacterial action. Furthermore, they have modified AG30/5C to enhance its stability and reduce its cost for clinical application in the treatment of ulcers. Finally, they have successfully produced SR-0379 as a multifunctional peptide.
SR-0379 has wound healing promotion functions such as granulation tissue formation (angiogenesis, proliferation) and remodeling (intensifying of tension for skin cleavage). SR-0379 has an α-helix structure with a number of hydrophobic and cationic amino acids. Antimicrobial peptides (AMPs) typically contain 20 – 60 amino acids, consisting of both cationic and hydrophobic amino acids. They show secondary structures such as α-helix and can kill a range of bacteria. Similarly, SR-0379 shows a broad spectrum for anti-microbial activity against various bacteria and fungi by disrupting membranes.
Now, we are developing SR-0379 as an intractable skin ulcer drug.