TAILIEUCHUNG - Báo cáo khoa học: Esculentin-1b(1–18) – a membrane-active antimicrobial peptide that synergizes with antibiotics and modifies the expression level of a limited number of proteins in Escherichia coli

Antimicrobial peptides constitute one of the main classes of molecular weapons deployed by the innate immune system of all multicellular organisms to resist microbial invasion. A good proportion of all antimi-crobial peptides currently known, numbering hundreds of molecules, have been isolated from frog skin. | Esculentin-1b 1-18 - a membrane-active antimicrobial peptide that synergizes with antibiotics and modifies the expression level of a limited number of proteins in Escherichia coli Ludovica Marcellini1 Marina Borro1 Giovanna Gentile1 Andrea C. Rinaldi2 Lorenzo Stella3 Pierpaolo Aimola4 Donatella Barra1 and Maria Luisa Mangoni1 1 Istituto Pasteur-Fondazione Cenci Bolognetti Dipartimento di Scienze Biochimiche Azienda Ospedaliera S. Andrea Universita La Sapienza Rome Italy 2 Dipartimento di Scienze e Tecnologie Biomediche Universita di Cagliari Monserrato Italy 3 Dipartimento di Scienze e Tecnologie Chimiche University di Roma Tor Vergata Rome Italy 4 Dipartimento di Biologia di Base ed Applicata Universita de L Aquila Italy Keywords frog skin antimicrobialpeptides Gram-negative bacteria mode of action peptide-membrane interaction proteomics Correspondence M. L. Mangoni Units di Diagnostica Molecolare Avanzata II Facolta di Medicina e Chirurgia Azienda Ospedaliera S. Andrea via di Grottarossa 1035-00189 Roma Italy Fax 39 06 33776664 Tel 39 06 33775457 E-mail Received 18 May 2009 revised 27 July 2009 accepted 4 August 2009 doi Antimicrobial peptides constitute one of the main classes of molecular weapons deployed by the innate immune system of all multicellular organisms to resist microbial invasion. A good proportion of all antimicrobial peptides currently known numbering hundreds of molecules have been isolated from frog skin. Nevertheless very little is known about the effect s and the mode s of action of amphibian antimicrobial peptides on intact bacteria especially when they are used at subinhibitory concentrations and under conditions closer to those encountered in vivo. Here we show that esculentin-1b 1-18 Esc 1-18 GIFSKLAGKKLKNL-LISG-NH2 a linear peptide encompassing the first 18 residues of the full-length esculentin-lb rapidly kills Escherichia coli at the minimal inhibitory concentration. The .

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