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izvor podataka: crosbi

Selective antimicrobial activity and mode of action of adepantins, glycine-rich peptide antibiotics based on anuran antimicrobial peptide sequences (CROSBI ID 191542)

Prilog u časopisu | izvorni znanstveni rad | međunarodna recenzija

Ilić, Nada ; Novković, Mario ; Guida, Filomena ; Xhindoli, Daniela ; Benincasa, Monica ; Tossi, Alesandro ; Juretić, Davor Selective antimicrobial activity and mode of action of adepantins, glycine-rich peptide antibiotics based on anuran antimicrobial peptide sequences // Biochimica et biophysica acta. Biomembranes, 1828 (2013), 3; 1004-1012. doi: 10.1016/j.bbamem.2012.11.017

Podaci o odgovornosti

Ilić, Nada ; Novković, Mario ; Guida, Filomena ; Xhindoli, Daniela ; Benincasa, Monica ; Tossi, Alesandro ; Juretić, Davor

engleski

Selective antimicrobial activity and mode of action of adepantins, glycine-rich peptide antibiotics based on anuran antimicrobial peptide sequences

A challenge when designing membrane-active peptide antibiotics with therapeutic potential is how to ensure a useful antibacterial activity whilst avoiding unacceptable cytotoxicity for host cells. Understanding their mode of interaction with membranes and the reasons underlying their ability to distinguish between bacterial and eukaryotic cytoplasmic cells is crucial for any rational attempt to improve this selectivity. We have approached this problem by analysing natural helical antimicrobial peptides of anuran origin, using a structure–activity database to determine an antimicrobial selectivity index (SI) relating theminimal inhibitory concentration against Escherichia coli to the haemolytic activity (SI=HC50/MIC). A parameter that correlated strongly with SI, derived from the lengthwise asymmetry of the peptides' hydrophobicity (sequencemoment), was then used in the “Designer” algorithm to propose novel, highly selective peptides. Amongst these are the ‘adepantins’, peptides rich in glycines and lysines that are highly selective for Gram- negative bacteria, have an exceptionally low haemolytic activity, and are less than 50% homologous to any other natural or synthetic antimicrobial peptide. In particular, they showed a very high SI for E. coli (up to 400) whilst maintaining an antimicrobial activity in the 0.5–4 μM range. Experiments with monomeric, dimeric and fluorescently labelled versions of the adepantins, using different bacterial strains, host cells and model membrane systems provided insight into their mechanism of action.

antimicrobial peptide; helical peptide; membranolytic; selectivity index

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Podaci o izdanju

1828 (3)

2013.

1004-1012

objavljeno

0005-2736

10.1016/j.bbamem.2012.11.017

Povezanost rada

Fizika, Kemija, Biologija

Poveznice
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