{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,20]],"date-time":"2026-08-20T16:20:03Z","timestamp":1787242803216,"version":"build-2736575974"},"reference-count":36,"publisher":"American Society for Microbiology","issue":"7","license":[{"start":{"date-parts":[[2005,7,1]],"date-time":"2005-07-01T00:00:00Z","timestamp":1120176000000},"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":[[2005,7]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    The synthetic peptides Lfpep and kaliocin-1 include the sequences from positions 18 to 40 and 153 to 183 of human lactoferrin, respectively. Lfpep is a cationic peptide with bactericidal and giardicidal effects, whereas kaliocin-1 is a novel bactericidal peptide that corresponds to a highly homologous sequence present in the transferrin family of proteins. Both peptides presented fungicidal activity against\n                    <jats:italic>Candida<\/jats:italic>\n                    spp., including fluconazole- and amphotericin B-resistant clinical isolates. Lfpep exhibited higher antifungal activity (8- to 30-fold) and salt resistance than kaliocin-1. The killing activity of Lfpep was mediated by its permeabilizing activity on\n                    <jats:italic>Candida albicans<\/jats:italic>\n                    cells, whereas kaliocin-1 was unable to disrupt the cytoplasmic membrane, as indicated by its inability to allow permeation of propidium iodide and the small amount of K\n                    <jats:sup>+<\/jats:sup>\n                    released. The amino acid sequence of kaliocin-1 includes the \u201cmultidimensional antimicrobial signature\u201d conserved in disulfide-containing antimicrobial peptides and a striking similarity to brevinin-1Sa, an antimicrobial peptide from frog skin secretions, exhibiting a \u201c\n                    <jats:italic>Rana<\/jats:italic>\n                    box\u201d-like sequence. These features may be of interest in the design of new antifungals.\n                  <\/jats:p>","DOI":"10.1128\/aac.49.7.2583-2588.2005","type":"journal-article","created":{"date-parts":[[2005,6,24]],"date-time":"2005-06-24T22:22:50Z","timestamp":1119651770000},"page":"2583-2588","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":55,"title":["Different Anti-\n                    <i>Candida<\/i>\n                    Activities of Two Human Lactoferrin-Derived Peptides, Lfpep and Kaliocin-1"],"prefix":"10.1128","volume":"49","author":[{"given":"Mo\u0301nica","family":"Viejo-Di\u0301az","sequence":"first","affiliation":[{"name":"Department of Functional Biology (Microbiology), Faculty of Medicine"},{"name":"Laboratory of Oral Microbiology, School of Stomatology, University of Oviedo, 33006 Oviedo, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mari\u0301a T.","family":"Andre\u0301s","sequence":"additional","affiliation":[{"name":"Laboratory of Oral Microbiology, School of Stomatology, University of Oviedo, 33006 Oviedo, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jose\u0301 F.","family":"Fierro","sequence":"additional","affiliation":[{"name":"Department of Functional Biology (Microbiology), Faculty of Medicine"},{"name":"Laboratory of Oral Microbiology, School of Stomatology, University of Oviedo, 33006 Oviedo, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0014-5793(99)01545-8"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.273.3.1640"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1016\/0167-4838(92)90346-F"},{"key":"e_1_3_2_5_2","first-page":"478","volume":"75","year":"1993","unstructured":"Bellamy, W. 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