Abstract
A family of peptides with broad-spectrum antimicrobial activity has been isolated from the skin of the African clawed frog Xenopus laevis. It consists of two closely related peptides that are each 23 amino acids and differ by two substitutions. These peptides are water soluble, nonhemolytic at their effective antimicrobial concentrations, and potentially amphiphilic. At low concentrations they inhibit growth of numerous species of bacteria and fungi and induce osmotic lysis of protozoa. The sequence of a partial cDNA of the precursor reveals that both peptides derive from a common larger protein. These peptides appear to represent a previously unrecognized class of vertebrate antimicrobial activities.
Keywords
XenopusAntimicrobial peptidesBiologyAntimicrobialFrog SkinAfrican clawed frogPeptide sequencePeptideComplementary DNABiochemistryAmino acidMicrobiologyChemistryGene
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Publication Info
- Year
- 1987
- Type
- article
- Volume
- 84
- Issue
- 15
- Pages
- 5449-5453
- Citations
- 2264
- Access
- Closed
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Cite This
M Zasloff
(1987).
Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor..
Proceedings of the National Academy of Sciences
, 84
(15)
, 5449-5453.
https://doi.org/10.1073/pnas.84.15.5449
Identifiers
- DOI
- 10.1073/pnas.84.15.5449