{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T03:07:20Z","timestamp":1791342440198,"version":"4.3.1"},"reference-count":0,"publisher":"National Academy of Sciences","issue":"12","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[1990,6]]},"abstract":"<jats:p>The D enantiomers of three naturally occurring antibiotics--cecropin A, magainin 2 amide, and melittin--were synthesized. In addition, the D enantiomers of two synthetic chimeric cecropin-melittin hybrid peptides were prepared. Each D isomer was shown by circular dichroism to be a mirror image of the corresponding L isomer in several solvent mixtures. In 20% hexafluoro-2-propanol the peptides contained 43-75% alpha-helix. The all-D peptides were resistant to enzymatic degradation. The peptides produced single-channel conductances in planar lipid bilayers, and the D and L enantiomers caused equivalent amounts of electrical conductivity. All of the peptides were potent antibacterial agents against representative Gram-negative and Gram-positive species. The D and L enantiomers of each peptide pair were equally active, within experimental error. Sheep erythrocytes were lysed by both D- and L-melittin but not by either isomer of cecropin A, magainin 2 amide, or the hybrids cecropin A-(1-13)-melittin-(1-13)-NH2 or cecropin A-(1-8)-melittin-(1-18)-NH2. The infectivity of the bloodstream form of the malaria parasite Plasmodium falciparum was also inhibited by the D and L hybrids. It is suggested that the mode of action of these peptides on the membranes of bacteria, erythrocytes, plasmodia, and artificial lipid bilayers may be similar and involves the formation of ion-channel pores spanning the membranes, but without specific interaction with chiral receptors or enzymes.<\/jats:p>","DOI":"10.1073\/pnas.87.12.4761","type":"journal-article","created":{"date-parts":[[2006,5,31]],"date-time":"2006-05-31T07:22:02Z","timestamp":1149060122000},"page":"4761-4765","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":579,"title":["All-D amino acid-containing channel-forming antibiotic peptides."],"prefix":"10.1073","volume":"87","author":[{"given":"D","family":"Wade","sequence":"first","affiliation":[{"name":"Rockefeller University, New York, NY 10021."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"A","family":"Boman","sequence":"additional","affiliation":[{"name":"Rockefeller University, New York, NY 10021."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"B","family":"W\u00e5hlin","sequence":"additional","affiliation":[{"name":"Rockefeller University, New York, NY 10021."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"C M","family":"Drain","sequence":"additional","affiliation":[{"name":"Rockefeller University, New York, NY 10021."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"D","family":"Andreu","sequence":"additional","affiliation":[{"name":"Rockefeller University, New York, NY 10021."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"H G","family":"Boman","sequence":"additional","affiliation":[{"name":"Rockefeller University, New York, NY 10021."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"R B","family":"Merrifield","sequence":"additional","affiliation":[{"name":"Rockefeller University, New York, NY 10021."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[1990,6]]},"container-title":["Proceedings of the National Academy of Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pnas.org\/doi\/pdf\/10.1073\/pnas.87.12.4761","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,4,13]],"date-time":"2022-04-13T12:49:17Z","timestamp":1649854157000},"score":1,"resource":{"primary":{"URL":"https:\/\/pnas.org\/doi\/full\/10.1073\/pnas.87.12.4761"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1990,6]]},"references-count":0,"journal-issue":{"issue":"12","published-print":{"date-parts":[[1990,6]]}},"alternative-id":["10.1073\/pnas.87.12.4761"],"URL":"https:\/\/doi.org\/10.1073\/pnas.87.12.4761","relation":{},"ISSN":["0027-8424","1091-6490"],"issn-type":[{"value":"0027-8424","type":"print"},{"value":"1091-6490","type":"electronic"}],"subject":[],"published":{"date-parts":[[1990,6]]},"assertion":[{"value":"1990-06-01","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}