Esculentin-1 is a potent anti-microbial peptide present in minute amounts in skin secretions of Rana esculenta. It contains 46 amino-acid residues and a C-terminal disulfide bridge. We have explored the possibility of producing analogues of this peptide by recombinant expression in Escherichia coli of a fusion protein which is sequestered in inclusion bodies. The peptide of interest has been inserted at the N-terminus of the protein, from which it can be released by cyanogen bromide cleavage. The anti-microbial activities of the recombinant peptide as well as that of a mutant linear form devoid of the disulfide bridge are presented. The recombinant analogues retain the biological activity of the natural peptide, as tested with an inhibition zone assay against a variety of microorganisms. However, experiments on the rate of bacterial killing show that gram-negative bacteria are more sensitive to the peptides than the gram-positive bacterium, the effect of the cyclic peptide being in all cases faster than that of the linear molecule. Moreover, the activity against gram-negative bacteria for both peptides is not affected by salts, whereas the activity against Staphylococcus aureus is lost at high salt concentration.

Expression and activity of cyclic and linear analogues of esculentin-1, an antimicrobial peptide from amphibian skin / Ponti, Donatella; Mignogna, Giuseppina; Mangoni, Maria Luisa; DE BIASE, Daniela; Simmaco, Maurizio; Barra, Donatella. - In: EUROPEAN JOURNAL OF BIOCHEMISTRY. - ISSN 0014-2956. - STAMPA. - 263(1999), pp. 921-927. [10.1046/j.1432-1327.1999.00597.x]

Expression and activity of cyclic and linear analogues of esculentin-1, an antimicrobial peptide from amphibian skin.

PONTI, Donatella;MIGNOGNA, Giuseppina;MANGONI, Maria Luisa;DE BIASE, Daniela;SIMMACO, Maurizio;BARRA, Donatella
1999

Abstract

Esculentin-1 is a potent anti-microbial peptide present in minute amounts in skin secretions of Rana esculenta. It contains 46 amino-acid residues and a C-terminal disulfide bridge. We have explored the possibility of producing analogues of this peptide by recombinant expression in Escherichia coli of a fusion protein which is sequestered in inclusion bodies. The peptide of interest has been inserted at the N-terminus of the protein, from which it can be released by cyanogen bromide cleavage. The anti-microbial activities of the recombinant peptide as well as that of a mutant linear form devoid of the disulfide bridge are presented. The recombinant analogues retain the biological activity of the natural peptide, as tested with an inhibition zone assay against a variety of microorganisms. However, experiments on the rate of bacterial killing show that gram-negative bacteria are more sensitive to the peptides than the gram-positive bacterium, the effect of the cyclic peptide being in all cases faster than that of the linear molecule. Moreover, the activity against gram-negative bacteria for both peptides is not affected by salts, whereas the activity against Staphylococcus aureus is lost at high salt concentration.
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/11573/241743
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