{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,15]],"date-time":"2026-10-15T03:22:04Z","timestamp":1792034524660,"version":"4.4.0"},"reference-count":53,"publisher":"American Society for Microbiology","issue":"9","license":[{"start":{"date-parts":[[1998,9,1]],"date-time":"1998-09-01T00:00:00Z","timestamp":904608000000},"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":[[1998,9]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    Human neutrophils contain two structurally distinct types of antimicrobial peptides, \u03b2-sheet defensins (HNP-1 to HNP-4) and the \u03b1-helical peptide LL-37. We used radial diffusion assays and an improved National Committee for Clinical Laboratory Standards-type broth microdilution assay to compare the antimicrobial properties of LL-37, HNP-1, and protegrin (PG-1). Although generally less potent than PG-1, LL-37 showed considerable activity (MIC, &lt;10 \u03bcg\/ml) against\n                    <jats:italic>Pseudomonas aeruginosa<\/jats:italic>\n                    ,\n                    <jats:italic>Salmonella typhimurium<\/jats:italic>\n                    ,\n                    <jats:italic>Escherichia coli<\/jats:italic>\n                    ,\n                    <jats:italic>Listeria monocytogenes<\/jats:italic>\n                    ,\n                    <jats:italic>Staphylococcus epidermidis<\/jats:italic>\n                    ,\n                    <jats:italic>Staphylococcus aureus<\/jats:italic>\n                    , and vancomycin-resistant enterococci, even in media that contained 100 mM NaCl. Certain organisms (methicillin-resistant\n                    <jats:italic>S. aureus<\/jats:italic>\n                    ,\n                    <jats:italic>Proteus mirabilis<\/jats:italic>\n                    , and\n                    <jats:italic>Candida albicans<\/jats:italic>\n                    ) were resistant to LL-37 in media that contained 100 mM NaCl but were susceptible in low-salt media.\n                    <jats:italic>Burkholderia cepacia<\/jats:italic>\n                    was resistant to LL-37, PG-1, and HNP-1 in low- or high-salt media. LL-37 caused outer and inner membrane permeabilization of\n                    <jats:italic>E. coli<\/jats:italic>\n                    ML-35p. Chromogenic\n                    <jats:italic>Limulus<\/jats:italic>\n                    assays revealed that LL-37 bound to\n                    <jats:italic>E. coli<\/jats:italic>\n                    O111:B4 lipopolysaccharide (LPS) with a high affinity and that this binding showed positive cooperativity (Hill coefficient = 2.02). Circular dichroism spectrometry disclosed that LL-37 underwent conformational change in the presence of lipid A, transitioning from a random coil to an \u03b1-helical structure. The broad-spectrum antimicrobial properties of LL-37, its presence in neutrophils, and its inducibility in keratinocytes all suggest that this peptide and its precursor (hCAP-18) may protect skin and other tissues from bacterial intrusions and LPS-induced toxicity. The potent activity of LL-37 against\n                    <jats:italic>P. aeruginosa<\/jats:italic>\n                    , including mucoid and antibiotic-resistant strains, suggests that it or related molecules might have utility as topical bronchopulmonary microbicides in cystic fibrosis.\n                  <\/jats:p>","DOI":"10.1128\/aac.42.9.2206","type":"journal-article","created":{"date-parts":[[2018,10,8]],"date-time":"2018-10-08T20:33:24Z","timestamp":1539030804000},"page":"2206-2214","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":675,"title":["Activities of LL-37, a Cathelin-Associated Antimicrobial Peptide of Human Neutrophils"],"prefix":"10.1128","volume":"42","author":[{"given":"Jeffrey","family":"Turner","sequence":"first","affiliation":[{"name":"<!--label omitted: 1-->Department of Medicine, Center for the Health Sciences, Los Angeles, California"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yoon","family":"Cho","sequence":"additional","affiliation":[{"name":"<!--label omitted: 1-->Department of Medicine, Center for the Health Sciences, Los Angeles, California"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nhu-Nguyen","family":"Dinh","sequence":"additional","affiliation":[{"name":"<!--label omitted: 1-->Department of Medicine, Center for the Health Sciences, Los Angeles, California"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alan J.","family":"Waring","sequence":"additional","affiliation":[{"name":"<!--label omitted: 1-->Department of Medicine, Center for the Health Sciences, Los Angeles, California"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Robert I.","family":"Lehrer","sequence":"additional","affiliation":[{"name":"<!--label omitted: 1-->Department of Medicine, Center for the Health Sciences, Los Angeles, California"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.92.1.195"},{"key":"e_1_3_2_3_2","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1002\/prot.340100206","article-title":"Side chain-backbone hydrogen bonding contributes to helix stability in peptides derived from an \u03b1-helical region of carboxypeptidase A.","volume":"10","author":"Bruch M. 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