{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,23]],"date-time":"2026-08-23T16:52:15Z","timestamp":1787503935545,"version":"build-2736575974"},"reference-count":31,"publisher":"Wiley","issue":"8","license":[{"start":{"date-parts":[[2019,3,20]],"date-time":"2019-03-20T00:00:00Z","timestamp":1553040000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["DFG ExC306"],"award-info":[{"award-number":["DFG ExC306"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004435","name":"Universidad de Navarra","doi-asserted-by":"publisher","award":["PIUNA\u2010P2011\u201017 and P2015\u201014"],"award-info":[{"award-number":["PIUNA\u2010P2011\u201017 and P2015\u201014"]}],"id":[{"id":"10.13039\/501100004435","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["febs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FEBS Journal"],"published-print":{"date-parts":[[2019,4]]},"abstract":"<jats:p>\n                    Increasing failure of conventional antibiotics to combat bacterial infections requires the urgent development of new antibacterial drugs; a promising class of new drugs based on antimicrobial peptides. Here, we studied the molecular interaction of polycationic synthetic antilipopolysaccharide peptides (\n                    <jats:styled-content style=\"fixed-case\">SALPs<\/jats:styled-content>\n                    ) with various gram\u2010negative and gram\u2010positive bacteria, including resistant strains. The analysis of antimicrobial activity by conventional techniques and atomic force microscopy showed a strict dependence on amino acid (aa) sequences, with the type of amino acid, its position within the primary structure, and the sequence length being critical parameters. By monitoring lipopolysaccharide (\n                    <jats:styled-content style=\"fixed-case\">LPS<\/jats:styled-content>\n                    )\u2010 or bacteria\u2010induced cytokine production in human mononuclear cells and whole blood, we found a direct link between the binding of the lead compound Pep19\u20102.5 to\n                    <jats:italic>Salmonella enterica<\/jats:italic>\n                    and the anti\u2010inflammatory activity of the peptide. Thermodynamic analysis of Pep19\u20102.5 binding to the bacterial cell envelope showed an exothermic reaction with saturation characteristics, whereas small\u2010angle X\u2010ray scattering data indicated a direct attachment of Pep19\u20102.5 to the bacterial cell envelope. This binding preferentially takes place to the\n                    <jats:styled-content style=\"fixed-case\">LPS<\/jats:styled-content>\n                    outer monolayer, as evidenced by the change in the\n                    <jats:styled-content style=\"fixed-case\">LPS<\/jats:styled-content>\n                    acyl chain and phosphate vibrational bands seen by Fourier\u2010transform infrared spectroscopy. We report here that the anti\u2010inflammatory activity of Pep19\u20102.5 is not only connected with neutralization of cell\u2010free bacterial toxins but also with a direct binding of the peptide to the outer leaflet of the bacterial outer membrane.\n                  <\/jats:p>","DOI":"10.1111\/febs.14805","type":"journal-article","created":{"date-parts":[[2019,3,7]],"date-time":"2019-03-07T04:05:43Z","timestamp":1551931543000},"page":"1576-1593","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":15,"title":["Antibacterial action of synthetic antilipopolysaccharide peptides (SALP) involves neutralization of both membrane\u2010bound and free toxins"],"prefix":"10.1111","volume":"286","author":[{"given":"Wilmar","family":"Correa","sequence":"first","affiliation":[{"name":"Division of Biophysics Forschungszentrum Borstel Leibniz Lungenzentrum Borstel 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