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Trichoplaxin — A new membrane-active antimicrobial peptide from placozoan cDNA (CROSBI ID 205604)

Prilog u časopisu | izvorni znanstveni rad | međunarodna recenzija

Simunić, Juraj ; Petrov, Dražen ; Bouceba, Tahar ; Kamech, Nédia ; Benincasa, Monica ; Juretić, Davor Trichoplaxin — A new membrane-active antimicrobial peptide from placozoan cDNA // Biochimica et biophysica acta. Biomembranes, 1838 (2014), 5; 1430-1438. doi: 10.1016/j.bbamem.2014.02.003

Podaci o odgovornosti

Simunić, Juraj ; Petrov, Dražen ; Bouceba, Tahar ; Kamech, Nédia ; Benincasa, Monica ; Juretić, Davor

engleski

Trichoplaxin — A new membrane-active antimicrobial peptide from placozoan cDNA

A method based on the use of signal peptide sequences from antimicrobial peptide (AMP) precursors was used to mine a placozoa expressed sequence tag database and identified a potential antimicrobial peptide from Trichoplax adhaerens. This peptide, with predicted sequence FFGRLKSVWSAVKHGWKAAKSR is the first AMP from a placozoan species, and was named trichoplaxin. It was chemically synthesized and its structural properties, biological activities and membrane selectivity were investigated. It adopts an α- helical structure in contact with membrane-like environments and is active against both Gram- negative and Gram-positive bacterial species (including MRSA), as well as yeasts from the Candida genus. The cytotoxic activity, as assessed by the haemolytic activity against rat erythrocytes, U937 cell permeabilization to propidium iodide and MCF7 cell mitochondrial activity, is significantly lower than the antimicrobial activity. In tests with membrane models, trichoplaxin shows high affinity for anionic prokaryote-like membranes with good fit in kinetic studies. Conversely, there is a low affinity for neutral eukaryote-like membranes and absence of a dose dependent response. With high selectivity for bacterial cells and no homologous sequence in the UniProt, trichoplaxin is a new potential lead compound for development of broad- spectrum antibacterial drugs.

antimicrobial peptide; EST database; Trichoplax adhaerens; selectivity index; surface plasmon resonance; peptide-membrane interaction

Highlights • First report of antimicrobial peptide from placozoa EST database • Broad activity spectrum against G − and G + bacteria, including MRSA • Low toxicity and high selectivity for prokaryotic- like membranes.

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Podaci o izdanju

1838 (5)

2014.

1430-1438

objavljeno

0005-2736

10.1016/j.bbamem.2014.02.003

Povezanost rada

Fizika, Kemija, Biologija

Poveznice
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