An atypical member of the brevinin-1 family of antimicrobial peptides isolated from the skin of the European frog Rana dalmatina

J. Michael Conlon; Bernhard Seidel; Per F. Nielsen

doi:10.1016/j.cca.2004.01.003

An atypical member of the brevinin-1 family of antimicrobial peptides isolated from the skin of the European frog Rana dalmatina

J. Michael Conlon
, Bernhard Seidel
, Per F. Nielsen

School of Biomedical Sciences

Research output: Contribution to journal › Article › peer-review

17 Citations (Scopus)

Abstract

A single peptide with antimicrobial activity was extracted from the skin of the European agile frog (R. dalmatina). The primary structure of this 17 amino-acid-residue peptide (ILPLLLGKVVCAITKKC) does not immediately suggest membership of any of the previously described families of antimicrobial peptides from ranid frogs. However, if it is assumed that the peptide has undergone several residue deletions during the course of speciation, it shows sequence similarity with peptides belonging to the widely distributed brevinin-1 family, particularly those isolated from the related species Rana temporaria. The minimum inhibitory concentration of the peptide, termed brevinin-1Da, against the Gram-positive bacterium Staphylococcus aureus was 7 μM and against the Gram-negative bacterium Escherichia coli was 30 μM.

Original language	English
Pages (from-to)	191-196
Number of pages	6
Journal	Comparative Biochemistry and Physiology - C Toxicology and Pharmacology
Volume	137
Issue number	2
DOIs	https://doi.org/10.1016/j.cca.2004.01.003
Publication status	Published (in print/issue) - Feb 2004

Funding

This work was supported by an Interdisciplinary Grant (03/12-8-03-01) and a Faculty Support Grant (NP/03/01) from the United Arab Emirates University. The authors thank Drs Mahendra Patel and Agnes Sonnevend for technical assistance in the project.

Funders
United Arab Emirates University

Keywords

Antimicrobial peptide
Brevinin-1
Frog skin
HPLC purification
Temporin

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10.1016/j.cca.2004.01.003

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abstract = "A single peptide with antimicrobial activity was extracted from the skin of the European agile frog (R. dalmatina). The primary structure of this 17 amino-acid-residue peptide (ILPLLLGKVVCAITKKC) does not immediately suggest membership of any of the previously described families of antimicrobial peptides from ranid frogs. However, if it is assumed that the peptide has undergone several residue deletions during the course of speciation, it shows sequence similarity with peptides belonging to the widely distributed brevinin-1 family, particularly those isolated from the related species Rana temporaria. The minimum inhibitory concentration of the peptide, termed brevinin-1Da, against the Gram-positive bacterium Staphylococcus aureus was 7 μM and against the Gram-negative bacterium Escherichia coli was 30 μM.",

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KW - Frog skin

KW - HPLC purification

KW - Temporin

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An atypical member of the brevinin-1 family of antimicrobial peptides isolated from the skin of the European frog Rana dalmatina

Abstract

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Keywords

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