In:
FEBS Letters, Wiley, Vol. 324, No. 2 ( 1993-06-14), p. 159-161
Abstract:
Three antimicrobial peptides were isolated from skin secretion of the European frog, Rana esculenta . Two of them show similarity to brevinin‐1 and brevinin‐2, respectively, two antimicrobial peptides recently isolated from a Japanese frog [Morikawa, N., Hagiwara, K. and Nakajima, T. (1992) Biochem. Biophys. Res. Commun. 189, 184‐190]. The third one, named esculentin, is 46 residues long and represents a different type of peptide. All these peptides have as a common motif an intramolecular disulfide bridge located at the COOH‐terminal end. The peptides from R . esculenta show distinctive antibacterial activity against representative Gram‐negative and Gram‐positive bacterial species. In particular, esculentin is the most active against Staphylococcus aureus , and has a much lower hemolytic activity.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1016/0014-5793(93)81384-C
Language:
English
Publisher:
Wiley
Publication Date:
1993
detail.hit.zdb_id:
1460391-3
SSG:
12
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