Amphibian antimicrobial peptides
| Brevenin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | Brevenin | ||||||||
| Pfam | PF03032 | ||||||||
| InterPro | IPR004275 | ||||||||
| OPM superfamily | 211 | ||||||||
| OPM protein | 2jpy | ||||||||
| |||||||||
Amphibian antimicrobial peptides are a family of highly potent antimicrobial peptides with a large spectrum of activity, which are synthesized by vertebrates as an efficient host-defence mechanism against invading microorganisms. A number of these defence peptides are secreted from the skin of frogs and other amphibians, including the opiate-like dermorphins and deltorphins, and antimicrobial dermaseptins, temporins, bombinins, magainin, pseudin, bombesins, and maculatins.[1][2]
References
[edit]- ^ Conlon JM, Kolodziejek J, Nowotny N (August 2009). "Antimicrobial peptides from the skins of North American frogs". Biochimica et Biophysica Acta (BBA) - Biomembranes. 1788 (8): 1556–63. doi:10.1016/j.bbamem.2008.09.018. PMID 18983817.
- ^ Haney EF, Hunter HN, Matsuzaki K, Vogel HJ (August 2009). "Solution NMR studies of amphibian antimicrobial peptides: linking structure to function?". Biochimica et Biophysica Acta (BBA) - Biomembranes. 1788 (8): 1639–55. doi:10.1016/j.bbamem.2009.01.002. PMID 19272309.