{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,29]],"date-time":"2026-05-29T21:27:24Z","timestamp":1780090044145,"version":"3.54.0"},"reference-count":32,"publisher":"American Society for Microbiology","issue":"9","license":[{"start":{"date-parts":[[2006,9,1]],"date-time":"2006-09-01T00:00:00Z","timestamp":1157068800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Antimicrob Agents Chemother"],"published-print":{"date-parts":[[2006,9]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Bacterial lipopolysaccharides (LPS) are important triggers of the widespread inflammatory response, which contributes to the development of multiple organ failure during sepsis. The helical 37-amino-acid-long human antimicrobial peptide LL-37 not only possesses a broad-spectrum antimicrobial activity but also binds and neutralizes LPS. However, the use of LL-37 in sepsis treatment is hampered by the fact that it is also cytotoxic. To find a less toxic analog of LL-37, we used in silico analysis to identify amphipathic helical regions of LL-37. A 21-amino-acid fragment (GKE) was synthesized, the biological actions of which were compared to those of two equally long peptides derived from the N and C termini of LL-37 as well as native LL-37. GKE displayed antimicrobial activity against\n            <jats:italic>Escherichia coli<\/jats:italic>\n            ,\n            <jats:italic>Pseudomonas aeruginosa<\/jats:italic>\n            ,\n            <jats:italic>Staphylococcus aureus<\/jats:italic>\n            ,\n            <jats:italic>Candida albicans<\/jats:italic>\n            , and\n            <jats:italic>Candida parapsilosis<\/jats:italic>\n            that was similar to or even stronger than LL-37. GKE, as well as the equally long control peptides, attracted granulocytes in a fashion similar to that of LL-37, while only GKE was as potent as LL-37 in inhibiting LPS-induced vascular nitric oxide production. GKE caused less hemolysis and apoptosis in human cultured smooth muscle cells than LL-37. In summary, we have identified an active domain of LL-37, GKE, which displays antimicrobial activity in vitro and LPS-binding activity similar to those of LL-37 but is less toxic. GKE therefore holds promise as a template for the development of peptide antibiotics for the treatment of sepsis.\n          <\/jats:p>","DOI":"10.1128\/aac.01583-05","type":"journal-article","created":{"date-parts":[[2006,8,28]],"date-time":"2006-08-28T18:10:56Z","timestamp":1156788656000},"page":"2983-2989","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":74,"title":["In Silico Identification and Biological Evaluation of Antimicrobial Peptides Based on Human Cathelicidin LL-37"],"prefix":"10.1128","volume":"50","author":[{"given":"Thorgerdur","family":"Sigurdardottir","sequence":"first","affiliation":[{"name":"Section of Anesthesiology and Intensive Care"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pia","family":"Andersson","sequence":"additional","affiliation":[{"name":"Section of Anesthesiology and Intensive 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