Please use this identifier to cite or link to this item: http://hdl.handle.net/2445/108113
Title: Evidence of protein adsorption in pegylated liposomes: Influence of liposomal decoration
Author: Sangrà, Marc
Estelrich i Latràs, Joan
Sabaté Lagunas, Raimon
Espargaró Colomé, Alba
Busquets i Viñas, Ma. Antonia
Keywords: Liposomes
Proteïnes
Fluorescència
Nanopartícules
Liposomes
Proteins
Fluorescence
Nanoparticles
Issue Date: 10-Feb-2017
Publisher: MDPI
Abstract: In order to contribute to a better knowledge of the events involved in the formation of the protein corona when nanoparticles (NPs) come in contact with proteins, we report a study about the changes on the physicochemical properties of pristine, PEGylated and Cyclic Arginine-Glycine-Aspartate peptide (RGD)-functionalized large unilamelar liposomes (LUVs) or magnetoliposomes (MLs) upon incubation with Bovine Serum Albumin (BSA). The main phospholipid component of both LUVs and MLs was L-α-phosphatydylcholine (PC) or 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) with 20% of cholesterol. The most obvious indication of the interaction of BSA-nanosystems is given by changes in the hydrodynamic diameter of the particles but other evidence is needed to corroborate the process. Our findings indicate that size modification is a process that is accomplished in few hours and that is strongly dependent not only on the surface decoration but also of the lipid composition of both LUVs and MLs. Fluorescence quenching experiments as well as cryogenic transmission electron microscopy (Cryo-TEM) images assessed these changes and confirmed that although each system has to be studied in a particular way, we can establish three distinctive features that turn into more reactive systems: (a) compositions containing PC compared with their DMPC counterparts; (b) the presence of PEG and/or RGD compared to the pristine counterparts; and (c) the presence of SPIONs: MLs show higher interaction than LUVs of the same lipid composition. Consequently, PEGylation (that is supposed to make stealth NPs) actually fails in preventing complete protein binding.
Note: Reproducció del document publicat a: https://doi.org/10.3390/nano7020037
It is part of: Nanomaterials, 2017, vol. 7, num. 2, p. 37-52
Related resource: https://doi.org/10.3390/nano7020037
URI: http://hdl.handle.net/2445/108113
ISSN: 2079-4991
Appears in Collections:Articles publicats en revistes (Farmàcia, Tecnologia Farmacèutica i Fisicoquímica)

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