{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,2]],"date-time":"2026-07-02T11:03:49Z","timestamp":1782990229752,"version":"3.54.5"},"reference-count":40,"publisher":"Wiley","issue":"9","license":[{"start":{"date-parts":[[2013,7,26]],"date-time":"2013-07-26T00:00:00Z","timestamp":1374796800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Journal of Peptide Science"],"published-print":{"date-parts":[[2013,9]]},"abstract":"<jats:p>Antimicrobial\u2010peptide\u2010based therapies could represent a reliable alternative to overcome antibiotic resistance, as they offer potential advantages such as rapid microbicidal activity and multiple activities against a broad spectrum of bacterial pathogens.<\/jats:p><jats:p>Three synthetic antimicrobial peptides (AMPs), AMP72, AMP126, and also AMP2041, designed by using <jats:italic>ad hoc<\/jats:italic> screening software developed <jats:italic>in house<\/jats:italic>, were synthesized and tested against nine reference strains. The peptides showed a partial <jats:italic>\u03b2<\/jats:italic>\u2010sheet structure in 10\u2010mM phosphate buffer. Low cytolytic activity towards both human cell lines (epithelial, endothelial, and fibroblast) and sheep erythrocytes was observed for all peptides. The antimicrobial activity was dose dependent with a minimum bactericidal concentration (MBC) ranging from 0.17 to 10.12\u2009\u03bcM (0.4\u201318.5\u2009\u00b5g\/ml) for Gram\u2010negative and 0.94 to 20.65\u2009\u03bcM (1.72\u201046.5\u2009\u00b5g\/ml) for Gram\u2010positive bacteria. Interestingly, in high\u2010salt environment, the antibacterial activity was generally maintained for Gram\u2010negative bacteria. All peptides achieved complete bacterial killing in 20\u2009min or less against Gram\u2010negative bacteria. A linear time\u2010dependent membrane permeabilization was observed for the tested peptides at 12.5\u2009\u00b5g\/ml. In a medium containing Mg<jats:sup>2+<\/jats:sup> and Ca<jats:sup>2+<\/jats:sup>, the peptide combination with EDTA restores the antimicrobial activity particularly for AMP2041. Moreover, in combination with anti\u2010infective agents (quinolones or aminoglycosides) known to bind divalent cation, AMP126 and AMP2041 showed additive activity in comparison with colistin.<\/jats:p><jats:p>Our results suggest the following: (i) there is excellent activity against Gram\u2010negative bacteria, (ii) there is low cytolytic activity, (iii) the presence of a chelating agent restores the antimicrobial activity in a medium containing Mg<jats:sup>2+<\/jats:sup> and Ca<jats:sup>2+<\/jats:sup>, and (iv) the MBC value of the combination AMPs\u2013conventional antibiotics was lower than the MBC of single agents alone. Copyright \u00a9 2013 European Peptide Society and John Wiley &amp; Sons, Ltd.<\/jats:p>","DOI":"10.1002\/psc.2532","type":"journal-article","created":{"date-parts":[[2013,7,26]],"date-time":"2013-07-26T12:41:38Z","timestamp":1374842498000},"page":"554-565","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":22,"title":["<i>In vitro<\/i> activity of novel <i>in silico<\/i>\u2010developed antimicrobial peptides against a panel of bacterial pathogens"],"prefix":"10.1002","volume":"19","author":[{"given":"A. A.","family":"Romani","sequence":"first","affiliation":[{"name":"Dipartimento di Medicina Clinica e Sperimentale Universit\u00e0 di Parma  Parma Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"M. 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