{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,16]],"date-time":"2026-03-16T11:47:15Z","timestamp":1773661635994,"version":"3.50.1"},"reference-count":47,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[1998,12,4]],"date-time":"1998-12-04T00:00:00Z","timestamp":912729600000},"content-version":"vor","delay-in-days":886,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Journal of Peptide Science"],"published-print":{"date-parts":[[1996,7]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>The design of cecropin\u2013melittin hybrid analogues is of interest due to the similarities in the structure of the antimicrobial peptides cecropin and melittin but differences in their lytic properties. We suspected that a hydrophobic residue in position 2 of milittin (Ile<jats:sup>8<\/jats:sup> in the hybrid) plays an important role in the activity of the 15\u2010residue hybrid, KWKLFKKIGAVLKVL\u2010NH<jats:sub>2<\/jats:sub>, [CA(1\u20137)M(2\u20139)NH<jats:sub>2<\/jats:sub>] and have now examined its role in the analogue toward five test bacteria. Deletion of Ile<jats:sup>8<\/jats:sup> reduced activity, and it was not restored by lengthening to 15 residues by addition of another threonine at the C\u2010terminus. Replacement of Ile<jats:sup>8<\/jats:sup> by a hydrophobic leucine maintained good activity and Ala<jats:sup>8<\/jats:sup> was equally active for four organisms, although less active against <jats:italic>Staphylococcus aureus<\/jats:italic>. Replacement by the hydrophilic Ser<jats:sup>8<\/jats:sup> strongly reduced potency against all five organisms. Deletion of Leu<jats:sup>15<\/jats:sup> decreased activity, but addition of Thr<jats:sup>16<\/jats:sup> maintained good activity. The presence of hydrophobic residues appears to have a significant effect on the process of antibacterial activity. These peptide analogues showed voltage\u2010dependent conductance changes and are capable of forming ion\u2010pores in planar lipid bilayers. The antibacterial action of the peptides is thought to be first an ionic interaction with the anionic phosphate groups of the membrane followed by interaction with the hydrocarbon core of the membrane and subsequent reorientation into amphipathic \u03b1\u2010helical peptides that form pores (ion\u2010channels), which span the membrane. The analogue also showed an increase in \u03b1\u2010helicity with an increase in hexafluoro 2\u2010propanol concentration.<\/jats:p>","DOI":"10.1002\/psc.63","type":"journal-article","created":{"date-parts":[[2005,5,31]],"date-time":"2005-05-31T11:40:51Z","timestamp":1117539651000},"page":"223-232","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":40,"title":["Hydrophobic Effects on Antibacterial and Channel\u2010forming Properties of Cecropin A\u2013Melittin Hybrids"],"prefix":"10.1002","volume":"2","author":[{"given":"Padmaja","family":"Juvvadi","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Satyanarayana","family":"Vunnam","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Elizabeth L.","family":"Merrifield","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Hans G.","family":"Boman","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"R. 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