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Combination of ellipsometry, laser scanning microscopy and Z-scan fluorescence correlation spectroscopy elucidating interaction of cryptdin-4 with supported phospholipid bilayers
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SYSNO ASEP 0311018 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Combination of ellipsometry, laser scanning microscopy and Z-scan fluorescence correlation spectroscopy elucidating interaction of cryptdin-4 with supported phospholipid bilayers Title Kombinace elipsometrie, laserové skenovací mikroskopie a Z-skenové fluorescenční korelační spektroskopie objasňuje interakci cryptdinu-4 s podporovanými fosfolipidovými dvojvrstvami Author(s) Miszta, Adam (UFCH-W)
Macháň, Radek (UFCH-W)
Benda, Aleš (UFCH-W) RID, ORCID
Ouellette, A. J. (US)
Hermens, W. Th. (NL)
Hof, Martin (UFCH-W) RID, ORCIDSource Title Journal of Peptide Science - ISSN 1075-2617
Roč. 14, č. 4 (2008), s. 503-509Number of pages 7 s. Language eng - English Country GB - United Kingdom Keywords cryptdin-4 ; megainin 2 ; supported phospholipid bilayers ; ellipsometry Subject RIV CF - Physical ; Theoretical Chemistry R&D Projects LC06063 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) GA203/05/2308 GA ČR - Czech Science Foundation (CSF) GD203/05/H001 GA ČR - Czech Science Foundation (CSF) CEZ AV0Z40400503 - UFCH-W (2005-2011) UT WOS 000254901300022 DOI 10.1002/psc.938 Annotation The present study has two main objectives. The first is to characterize antimicrobial peptide (AMP) cryptdin-4 (Crp-4) 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 Z-scan fluorescence correlation spectroscopy (FCS) to acquire comprehensive information on mechanisms of AMP interactions with supported phospholipid bilayers (SPBs) - a popular model of biological membranes. LSM shows appearance of inhomogencities in spatial distribution of lipids in the bilayer after treatment with Crp-4. Ellipsometric measurements show that binding of Crp-4 does not significantly change the lipid structure of the bilayer (increase in adsorbed mass without a change in thickness of adsorbed layer). Furthermore, Crp-4 slows the lateral diffusion of lipids within the membrane as shown by Z-scan FCS. Workplace J. Heyrovsky Institute of Physical Chemistry Contact Michaela Knapová, michaela.knapova@jh-inst.cas.cz, Tel.: 266 053 196 Year of Publishing 2009
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