Interaction of the pitavastatin with model membranes |
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Authors: | Guzel S Shurshalova Holger A Scheidt Markus Fischer Daniel Huster Albert V Aganov Vladimir V Klochkov |
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Institution: | 1. Institute for Medical Physics and Biophysics, Leipzig University, Härtelstr. 16-18, D-04107 Leipzig, Germany;2. Institute of Physics, Kazan (Volga Region) Federal University, 18 Kremlevskaya St., 420008 Kazan, Russian Federation |
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Abstract: | Pitavastatin is a statin drug that, by competitively inhibiting 3-hydroxy-3-methylglutaryl-coenzyme A reductase, can lower serum cholesterol levels of low-density lipoprotein (LDL) accompanied by side effects due to pleiotropic effects leading to statin intolerance. These effects can be explained by the lipophilicity of statins, which creates membrane affinity and causes statin localization in cellular membranes. In the current report, the interaction of pitavastatin with POPC model membranes and its influence on the membrane structure were investigated using 1H, 2H and 31P solid-state NMR spectroscopy. Our experiments show the average localization of pitavastatin at the lipid/water interface of the membrane, which is biased towards the hydrocarbon core in comparison to other statin molecules. The membrane binding of pitavastatin also introduced an isotropic component into the 31P NMR powder spectra, suggesting that some of the lamellar POPC molecules are converted into highly curved structures. |
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Keywords: | Statin Model membrane POPC bilayer MAS NMR Order parameters |
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