LNP shell structure and controlling ApoE lipid removal
Apolipoproteins are the amphipathic proteins that enable the transport of fat in the body. Apolipoprotein E (ApoE) is an important protein mainly present in HDL that enables HDL recognition in the liver and fat removal from the body. ApoE is the main component of the protein corona present in lipidic nanoparticles such as liposomes and lipid-based nanoparticles (LNPs). Using neutron reflectometry (NR), we demonstrated that ApoE selectively removed saturated lipids and had a lower affinity for unsaturated lipids or cholesterol molecules. ApoE binds to LNPs is the main reason why LNPs are cleared from the body via the liver, and therefore blocking ApoE binding to LNPs seems a logical way to improve LNP efficiency and enable organ targeting. It has been shown that substitution of cholesterol by a plant sterol increases LNP efficiency and modulated LNP morphology. Among plant sterols, campesterol is of special interest since its ingestion lowers plasma cholesterol levels. Neutron reflectivity is a key technique to get determine the structure and composition of lipid bilayer matching the shell of LNPs upon binding to ApoE.
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The recommended format for citing this dataset in a research publication is in the following format:
CARDENAS; DRDANOVSKI Jovana; FELDERER Birgit; GUTFREUND Philipp and KYZYMA Olena. (2025). LNP shell structure and controlling ApoE lipid removal. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.9-13-1160
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