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    Cyclosporin A distribution in cholesterol-sphingomyelin artificial membranes modeled as Langmuir monolayers

    Year: 2018

    Journal: Colloid Surf. B-Biointerfaces, Volume 166, JUN 1, page 286–294

    Authors: Wnetrzak, Anita; Makyla-Juzak, Katarzyna; Chachaj-Brekiesz, Anna; Lipiec, Ewelina; Romeu, Nuria Vila; Dynarowicz-Latka, Patrycja

    Organizations: European Regional Development Fund [POIG.02.01.00-12-023/08]; Matopolska Regional Operational Programme Measure 5.1 Krakow Metropolitan Area as an important hub of the European Research Area [MRPO.05.01.00-12-013/15]; National Science Center of the Republic of Poland (Narodowe Centrum Nauki-NCN) [2014/13/D/NZ1/01014]

    Keywords: Cyclosporin A; Langmuir monolayers; Sphingomyelin-cholesterol model membranes

    Cyclosporin A (CsA), a hydrophobic peptide, mainly known for its immunosuppressant properties, has shown a broad range of biological activities, including antimalarial action. Since CsA was found to be active on membrane level, it was subjected for investigations involving membrane models. Our former studies on interactions between CsA and different membrane lipids using Langmuir monolayer technique indicated its affinity for sphingomyelin (SM). Inspired by this finding we have extended our experiments on multicomponent systems and performed systematic investigations of CsA behavior towards artificial membranes containing different mutual proportion of sphingomyelin and cholesterol (Chol). Langmuir monolayer results have been complemented with in-situ films structure visualization applying Brewster angle microscopy (BAM) and, after films transfer onto solid support, atomic force microscopy (AFM). Our results show that cyclosporin A introduced to SM:Chol mixed monolayers distributes differently, depending on SM-to-Chol proportion. In raft-mimicking (2:1) stoichiometry, even distribution of the drug within SM:Chol matrix was observed. However, in SM:Chol model membranes of different proportion (3:1; 1:1; 1:2), containing either the excess of unbound sphingomyelin or cholesterol in addition to model lipid raft domains, introduction of CsA induced a phase separation. (C) 2018 Elsevier B.V. All rights reserved.
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