{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,19]],"date-time":"2026-09-19T03:50:47Z","timestamp":1789789847238,"version":"4.0.1"},"reference-count":82,"publisher":"MDPI AG","issue":"10","license":[{"start":{"date-parts":[[2023,9,30]],"date-time":"2023-09-30T00:00:00Z","timestamp":1696032000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Italian Cystic Fibrosis Research Foundation with the contribution of \u201cDelegazione FFC di Imola e Romagna\u201d","award":["FFC#18\/2018"],"award-info":[{"award-number":["FFC#18\/2018"]}]},{"name":"Italian Cystic Fibrosis Research Foundation with the contribution of \u201cDelegazione FFC di Imola e Romagna\u201d","award":["PRIN 2020AEX4TA"],"award-info":[{"award-number":["PRIN 2020AEX4TA"]}]},{"name":"Italian Cystic Fibrosis Research Foundation with the contribution of \u201cDelegazione FFC di Imola e Romagna\u201d","award":["P2022ZBNC2"],"award-info":[{"award-number":["P2022ZBNC2"]}]},{"name":"University of Salerno, FARB","award":["FFC#18\/2018"],"award-info":[{"award-number":["FFC#18\/2018"]}]},{"name":"University of Salerno, FARB","award":["PRIN 2020AEX4TA"],"award-info":[{"award-number":["PRIN 2020AEX4TA"]}]},{"name":"University of Salerno, FARB","award":["P2022ZBNC2"],"award-info":[{"award-number":["P2022ZBNC2"]}]},{"name":"Ministero dell\u2019Universit\u00e0 e della Ricerca (MUR)","award":["FFC#18\/2018"],"award-info":[{"award-number":["FFC#18\/2018"]}]},{"name":"Ministero dell\u2019Universit\u00e0 e della Ricerca (MUR)","award":["PRIN 2020AEX4TA"],"award-info":[{"award-number":["PRIN 2020AEX4TA"]}]},{"name":"Ministero dell\u2019Universit\u00e0 e della Ricerca (MUR)","award":["P2022ZBNC2"],"award-info":[{"award-number":["P2022ZBNC2"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Pharmaceuticals"],"abstract":"<jats:p>Cationic antimicrobial peptides (CAMPs) are powerful molecules with antimicrobial, antibiofilm and endotoxin-scavenging activities. These properties make CAMPs very attractive drugs in the face of the rapid increase in multidrug-resistant (MDR) pathogens, but they are limited by their susceptibility to proteolytic degradation. An intriguing solution to this issue could be the development of functional mimics of CAMPs with structures that enable the evasion of proteases. Peptoids (N-substituted glycine oligomers) are an important class of peptidomimetics with interesting benefits: easy synthetic access, intrinsic proteolytic stability and promising bioactivities. Here, we report the characterization of P13#1, a 13-residue peptoid specifically designed to mimic cathelicidins, the best-known and most widespread family of CAMPs. P13#1 showed all the biological activities typically associated with cathelicidins: bactericidal activity over a wide spectrum of strains, including several ESKAPE pathogens; the ability to act in combination with different classes of conventional antibiotics; antibiofilm activity against preformed biofilms of Pseudomonas aeruginosa, comparable to that of human cathelicidin LL-37; limited toxicity; and an ability to inhibit LPS-induced proinflammatory effects which is comparable to that of \u201cthe last resource\u201d antibiotic colistin. We further studied the interaction of P13#1 with SDS, LPSs and bacterial cells by using a fluorescent version of P13#1. Finally, in a subcutaneous infection mouse model, it showed antimicrobial and anti-inflammatory activities comparable to ampicillin and gentamicin without apparent toxicity. The collected data indicate that P13#1 is an excellent candidate for the formulation of new antimicrobial therapies.<\/jats:p>","DOI":"10.3390\/ph16101386","type":"journal-article","created":{"date-parts":[[2023,10,1]],"date-time":"2023-10-01T16:57:06Z","timestamp":1696179426000},"page":"1386","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":16,"title":["The Antimicrobial, Antibiofilm and Anti-Inflammatory Activities of P13#1, a Cathelicidin-like Achiral Peptoid"],"prefix":"10.3390","volume":"16","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-6686-7657","authenticated-orcid":false,"given":"Valeria","family":"Cafaro","sequence":"first","affiliation":[{"name":"Department of Biology, University of Naples Federico II, 80126 Naples, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2360-300X","authenticated-orcid":false,"given":"Andrea","family":"Bosso","sequence":"additional","affiliation":[{"name":"Department of Biology, University of Naples Federico II, 80126 Naples, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ilaria","family":"Di Nardo","sequence":"additional","affiliation":[{"name":"Department of Biology, University of Naples Federico II, 80126 Naples, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9246-5523","authenticated-orcid":false,"given":"Assunta","family":"D\u2019Amato","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Biology \u201cA. Zambelli\u201d, University of Salerno, 84084 Fisciano, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0369-0102","authenticated-orcid":false,"given":"Irene","family":"Izzo","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Biology \u201cA. Zambelli\u201d, University of Salerno, 84084 Fisciano, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8121-9463","authenticated-orcid":false,"given":"Francesco","family":"De Riccardis","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Biology \u201cA. Zambelli\u201d, University of Salerno, 84084 Fisciano, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marialuisa","family":"Siepi","sequence":"additional","affiliation":[{"name":"Department of Biology, University of Naples Federico II, 80126 Naples, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rosanna","family":"Culurciello","sequence":"additional","affiliation":[{"name":"Department of Biology, University of Naples Federico II, 80126 Naples, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nunzia","family":"D\u2019Urzo","sequence":"additional","affiliation":[{"name":"Department of Biology, University of Naples Federico II, 80126 Naples, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Emiliano","family":"Chiarot","sequence":"additional","affiliation":[{"name":"GSK, 53100 Siena, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Antonina","family":"Torre","sequence":"additional","affiliation":[{"name":"GSK, 53100 Siena, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3652-8865","authenticated-orcid":false,"given":"Elio","family":"Pizzo","sequence":"additional","affiliation":[{"name":"Department of Biology, University of Naples Federico II, 80126 Naples, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4298-4015","authenticated-orcid":false,"given":"Marcello","family":"Merola","sequence":"additional","affiliation":[{"name":"Department of Biology, University of Naples Federico II, 80126 Naples, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Eugenio","family":"Notomista","sequence":"additional","affiliation":[{"name":"Department of Biology, University of Naples Federico II, 80126 Naples, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2023,9,30]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"440","DOI":"10.4161\/viru.1.5.12983","article-title":"Antimicrobial peptides: The ancient arm of the human immune system","volume":"1","author":"Wiesner","year":"2010","journal-title":"Virulence"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"443","DOI":"10.1016\/j.it.2014.07.004","article-title":"Host defense peptides: Front-line immunomodulators","volume":"35","author":"Mansour","year":"2014","journal-title":"Trends Immunol."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"eaan4044","DOI":"10.1126\/scitranslmed.aan4044","article-title":"The antimicrobial peptide SAAP-148 combats drug-resistant bacteria and biofilms","volume":"10","author":"Riool","year":"2018","journal-title":"Sci. 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