{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,30]],"date-time":"2026-04-30T06:43:13Z","timestamp":1777531393965,"version":"3.51.4"},"reference-count":54,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2002,6,25]],"date-time":"2002-06-25T00:00:00Z","timestamp":1024963200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["The Journal of Peptide Research"],"published-print":{"date-parts":[[2002,7]]},"abstract":"<jats:p><jats:bold>Abstract:<\/jats:bold> CRAMP was identified from a cDNA clone derived from mouse femoral marrow cells as a member of cathelicidin\u2010derived antimicrobial peptides. This peptide shows potent antimicrobial activity against gram\u2010positive and gram\u2010negative bacteria but no hemolytic activity against human erythrocytes. CRAMP was known to cause rapid permeabilization of the inner membrane of <jats:italic>Escherichia coli.<\/jats:italic> In this study, the structure of CRAMP in TFE\/H<jats:sub>2<\/jats:sub>O (1\u200a:\u200a1, v\/v) solution was determined by CD and NMR spectroscopy. CD spectra showed that CRAMP adopts a mainly \u03b1\u2010helical conformation in TFE\/H<jats:sub>2<\/jats:sub>O solution, DPC micelles, SDS micelles and liposomes, whereas it has a random structure in aqueous solution. The tertiary structure of CRAMP in TFE\/H<jats:sub>2<\/jats:sub>O (1\u200a:\u200a1, v\/v), as determined by NMR spectroscopy, consists of two amphipathic \u03b1\u2010helices from Leu<jats:sup>4<\/jats:sup> to Lys<jats:sup>10<\/jats:sup> and from Gly<jats:sup>16<\/jats:sup> to Leu<jats:sup>33<\/jats:sup>. These two helices are connected by a flexible region from Gly<jats:sup>11<\/jats:sup> to Gly<jats:sup>16<\/jats:sup>. Previous analysis of series of fragments composed of various portion of CRAMP revealed that an 18\u2010residue fragment with the sequence from Gly<jats:sup>16<\/jats:sup> to Leu<jats:sup>33<\/jats:sup> was found to retain antibacterial activity. Therefore, the amphipathic \u03b1\u2010helical region from Gly<jats:sup>16<\/jats:sup> to Leu<jats:sup>33<\/jats:sup> of CRAMP plays important roles in spanning the lipid bilayers as well as its antibiotic activity. Based on this structure, novel antibiotic peptides having strong antibiotic activity, with no hemolytic effect will be developed.<\/jats:p>","DOI":"10.1034\/j.1399-3011.2002.01968.x","type":"journal-article","created":{"date-parts":[[2003,3,12]],"date-time":"2003-03-12T08:42:03Z","timestamp":1047458523000},"page":"1-9","source":"Crossref","is-referenced-by-count":33,"title":["Solution structure of a cathelicidin\u2010derived antimicrobial peptide, CRAMP as determined by NMR 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