Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor - PubMed (original) (raw)

Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor

M Zasloff. Proc Natl Acad Sci U S A. 1987 Aug.

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.

PubMed Disclaimer

Similar articles

Cited by

References

    1. Nature. 1970 Aug 15;227(5259):680-5 - PubMed
    1. Cell. 1986 Aug 1;46(3):377-85 - PubMed
    1. Anal Biochem. 1976 May 7;72:248-54 - PubMed
    1. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463-7 - PubMed
    1. Nature. 1979 Feb 8;277(5696):491-2 - PubMed

MeSH terms

Substances

LinkOut - more resources