{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,15]],"date-time":"2025-10-15T17:15:15Z","timestamp":1760548515865,"version":"3.37.3"},"reference-count":32,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2007,11,12]],"date-time":"2007-11-12T00:00:00Z","timestamp":1194825600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"name":"The National Research Center","award":["LC06063"],"award-info":[{"award-number":["LC06063"]}]},{"DOI":"10.13039\/501100001824","name":"Grant Agency of the Czech Republic","doi-asserted-by":"crossref","award":["203\/05\/H001"],"award-info":[{"award-number":["203\/05\/H001"]}],"id":[{"id":"10.13039\/501100001824","id-type":"DOI","asserted-by":"crossref"}]},{"name":"NIH","award":["AI059346","DK044632"],"award-info":[{"award-number":["AI059346","DK044632"]}]},{"name":"Human Fronteirs Science Program"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Journal of Peptide Science"],"published-print":{"date-parts":[[2008,4]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>The present study has two main objectives. The first is to characterize antimicrobial peptide (AMP) cryptdin\u20104 (Crp\u20104) interactions with biological membranes and to compare those interactions with those of magainin 2. The second is to combine the complementary experimental approaches of laser scanning microscopy (LSM), ellipsometry, and <jats:italic>Z<\/jats:italic>\u2010scan fluorescence correlation spectroscopy (FCS) to acquire comprehensive information on mechanisms of AMP interactions with supported phospholipid bilayers (SPBs)\u2014a popular model of biological membranes. LSM shows appearance of inhomogeneities in spatial distribution of lipids in the bilayer after treatment with Crp\u20104. Ellipsometric measurements show that binding of Crp\u20104 does not significantly change the lipid structure of the bilayer (increase in adsorbed mass without a change in thickness of adsorbed layer). Furthermore, Crp\u20104 slows the lateral diffusion of lipids within the membrane as shown by <jats:italic>Z<\/jats:italic>\u2010scan FCS. All changes of the bilayer induced by Crp\u20104 can be partially reversed by flushing the sample with excess of buffer. Bilayer interactions of magainin 2 are significantly different, causing large loss of lipids and extensive damage to the bilayer. It seems likely that differences in peptide mode of action, readily distinguished using these combined experimental methods, are related to the distinctive \u03b2\u2010sheet and \u03b1\u2010helical structures of the respective peptides. Copyright \u00a9 2007 European Peptide Society and John Wiley &amp; Sons, Ltd.<\/jats:p>","DOI":"10.1002\/psc.938","type":"journal-article","created":{"date-parts":[[2007,11,12]],"date-time":"2007-11-12T11:19:30Z","timestamp":1194866370000},"page":"503-509","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":22,"title":["Combination of ellipsometry, laser scanning microscopy and <i>Z<\/i>\u2010scan fluorescence correlation spectroscopy elucidating interaction of cryptdin\u20104 with supported phospholipid bilayers"],"prefix":"10.1002","volume":"14","author":[{"given":"Adam","family":"Miszta","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Radek","family":"Mach\u00e1\u0148","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ale\u0161","family":"Benda","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Andre J.","family":"Ouellette","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Wim Th.","family":"Hermens","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Martin","family":"Hof","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2007,11,12]]},"reference":[{"key":"e_1_2_1_2_2","doi-asserted-by":"publisher","DOI":"10.1038\/415389a"},{"key":"e_1_2_1_3_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0005-2736(99)00202-3"},{"key":"e_1_2_1_4_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.eururo.2005.12.043"},{"key":"e_1_2_1_5_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.88.9.3792"},{"key":"e_1_2_1_6_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0005-2736(99)00205-9"},{"key":"e_1_2_1_7_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0005-2736(99)00200-X"},{"key":"e_1_2_1_8_2","doi-asserted-by":"publisher","DOI":"10.1529\/biophysj.105.073890"},{"key":"e_1_2_1_9_2","doi-asserted-by":"publisher","DOI":"10.1096\/fasebj.10.11.8836041"},{"key":"e_1_2_1_10_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M212115200"},{"key":"e_1_2_1_11_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M310251200"},{"key":"e_1_2_1_12_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0005-2736(97)00051-5"},{"key":"e_1_2_1_13_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi0267846"},{"key":"e_1_2_1_14_2","doi-asserted-by":"publisher","DOI":"10.1046\/j.1432-1033.2003.03840.x"},{"key":"e_1_2_1_15_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0005-2736(99)00201-1"},{"key":"e_1_2_1_16_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi051684w"},{"key":"e_1_2_1_17_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.peptides.2003.08.020"},{"key":"e_1_2_1_18_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M602041200"},{"key":"e_1_2_1_19_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M210600200"},{"key":"e_1_2_1_20_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.286.5437.113"},{"key":"e_1_2_1_21_2","first-page":"521","article-title":"Structure, function, and membrane integration of defensins","volume":"5","author":"White SH","year":"1995","journal-title":"Curr. 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