Jump to content

Amphibian antimicrobial peptides

From Wikipedia, the free encyclopedia
Brevenin
Identifiers
SymbolBrevenin
PfamPF03032
InterProIPR004275
OPM superfamily211
OPM protein2jpy
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

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]
  1. ^ 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.
  2. ^ 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.
This article incorporates text from the public domain Pfam and InterPro: IPR004275