{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,5]],"date-time":"2026-01-05T04:08:03Z","timestamp":1767586083756},"reference-count":58,"publisher":"Wiley","issue":"5","license":[{"start":{"date-parts":[[2003,3,28]],"date-time":"2003-03-28T00:00:00Z","timestamp":1048809600000},"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":[[2003,5]]},"abstract":"<jats:p><jats:bold>Abstract:<\/jats:bold>  The hexapeptide Ac\u2010RRWWRF\u2010NH<jats:sub>2<\/jats:sub> has earlier been identified as a potent antimicrobial peptide by screening synthetic combinatorial hexapeptide libraries. In this study, it was found that this peptide had a large influence on the thermotropic phase behavior of model membranes containing the negatively charged headgroup phosphatidylglycerol, a major component of bacterial membranes. In contrast, differential scanning calorimetry showed that it had little effect on model membranes containing the zwitterionic phosphatidylcholine headgroup, the main component of erythrocyte membranes. This behavior is consistent with its biological activity and with its affinity to these membranes as determined by titration calorimetry, implying that peptide\u2013lipid interactions play an important role in this process. The structure of this peptide bound to membrane\u2010mimetic sodium dodecyl sulfate (SDS) and dodecylphosphocholine micelles has been determined using conventional two\u2010dimensional nuclear magnetic resonance methods. It forms a marked amphipathic structure in SDS with its hydrophobic residues on one side of the structure and with the positively charged residues on the other side. This amphipathic structure may allow this peptide to penetrate deeper into the interfacial region of negatively charged membranes, leading to local membrane destabilization. Knowledge about the importance of electrostatic interactions of Arg and the role of Trp residues as a membrane interface anchor will provide insight into the future design of potent antimicrobial peptidomimetics.<\/jats:p>","DOI":"10.1034\/j.1399-3011.2003.00050.x","type":"journal-article","created":{"date-parts":[[2010,11,12]],"date-time":"2010-11-12T17:43:30Z","timestamp":1289583810000},"page":"219-229","source":"Crossref","is-referenced-by-count":85,"title":["The structure of the antimicrobial peptide Ac\u2010RRWWRF\u2010NH<sub>2<\/sub> bound to micelles and its interactions with phospholipid bilayers"],"prefix":"10.1034","volume":"61","author":[{"given":"W.","family":"Jing","sequence":"first","affiliation":[]},{"given":"H.N.","family":"Hunter","sequence":"additional","affiliation":[]},{"given":"J.","family":"Hagel","sequence":"additional","affiliation":[]},{"given":"H.J.","family":"Vogel","sequence":"additional","affiliation":[]}],"member":"311","published-online":{"date-parts":[[2008,12,5]]},"reference":[{"key":"e_1_2_16_2_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.iy.13.040195.000425"},{"key":"e_1_2_16_3_2","doi-asserted-by":"publisher","DOI":"10.1016\/0952-7915(92)90115-U"},{"key":"e_1_2_16_4_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.mi.49.100195.001425"},{"key":"e_1_2_16_5_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0167-7799(97)01156-6"},{"key":"e_1_2_16_6_2","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1002\/bip.360370306","article-title":"review of the utility of soluble peptide combinatorial libraries","volume":"37","author":"Pinilla C.","journal-title":"Biopolymers"},{"key":"e_1_2_16_7_2","doi-asserted-by":"publisher","DOI":"10.1016\/0167-7799(96)80922-X"},{"key":"e_1_2_16_8_2","doi-asserted-by":"publisher","DOI":"10.1002\/(SICI)1097-0282(1998)47:6<451::AID-BIP4>3.0.CO;2-F"},{"key":"e_1_2_16_9_2","doi-asserted-by":"publisher","DOI":"10.1006\/bbrc.1998.8159"},{"key":"e_1_2_16_10_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0005-2736(99)00198-4"},{"key":"e_1_2_16_11_2","first-page":"117","volume-title":"Gram\u2010positive bacteria, in Microbial lipids","author":"O'Leary W.M.","year":"1988"},{"key":"e_1_2_16_12_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.bi.48.070179.000403"},{"key":"e_1_2_16_13_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0005-2736(99)00004-8"},{"key":"e_1_2_16_14_2","doi-asserted-by":"publisher","DOI":"10.1021\/j100546a014"},{"key":"e_1_2_16_15_2","doi-asserted-by":"publisher","DOI":"10.1016\/0006-291X(83)91225-1"},{"key":"e_1_2_16_16_2","doi-asserted-by":"publisher","DOI":"10.1016\/0022-2364(83)90226-3"},{"key":"e_1_2_16_17_2","doi-asserted-by":"publisher","DOI":"10.1063\/1.438208"},{"key":"e_1_2_16_18_2","doi-asserted-by":"publisher","DOI":"10.1007\/BF00197809"},{"key":"e_1_2_16_19_2","doi-asserted-by":"publisher","DOI":"10.1007\/BF00404272"},{"key":"e_1_2_16_20_2","first-page":"905","article-title":"Crystallography and NMR system: a new software suite for macromolecular structure determination","volume":"54","author":"Brunger A.T.","year":"1998","journal-title":"Acta Crystal."},{"key":"e_1_2_16_21_2","doi-asserted-by":"publisher","DOI":"10.1006\/jmbi.1994.0053"},{"key":"e_1_2_16_22_2","doi-asserted-by":"publisher","DOI":"10.1016\/0009-3084(82)90053-6"},{"key":"e_1_2_16_23_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0006-3495(97)78712-5"},{"key":"e_1_2_16_24_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1432-1033.1997.00938.x"},{"key":"e_1_2_16_25_2","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1007\/978-1-4757-3061-6","volume-title":"Principles of Fluorescence Spectroscopy","author":"Lakowicz J.R.","year":"1999"},{"key":"e_1_2_16_26_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0076-6879(94)39020-7"},{"key":"e_1_2_16_27_2","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1126\/science.276.5309.131","article-title":"transmembrane helix dimer: structure and implications","volume":"276","author":"MacKenzie K.R.","journal-title":"Science"},{"key":"e_1_2_16_28_2","first-page":"845","article-title":"NMR and membrane proteins","volume":"4","author":"Opella S.J.","year":"1997","journal-title":"Nat. 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