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Nanomaterials 2017, 7(2), 37; doi:10.3390/nano7020037

Evidence of Protein Adsorption in Pegylated Liposomes: Influence of Liposomal Decoration

1
Department of Pharmacy, Pharmaceutical Technology and Physical Chemistry, Faculty of Pharmacy and Food Sciences, University of Barcelona, Avda. Joan XXIII, 27-31, 08028 Barcelona, Spain
2
Nanoscience and Nanotechnology Institute (IN2UB), Avda. Joan XXIII, 27-31, 08028 Barcelona, Spain
*
Author to whom correspondence should be addressed.
Academic Editor: Thomas Nann
Received: 10 December 2016 / Revised: 24 January 2017 / Accepted: 3 February 2017 / Published: 10 February 2017
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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. View Full-Text
Keywords: magnetoliposomes; liposomes; BSA; protein corona; fluorescence anisotropy; fluorescence quenching magnetoliposomes; liposomes; BSA; protein corona; fluorescence anisotropy; fluorescence quenching
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Sangrà, M.; Estelrich, J.; Sabaté, R.; Espargaró, A.; Busquets, M.A. Evidence of Protein Adsorption in Pegylated Liposomes: Influence of Liposomal Decoration. Nanomaterials 2017, 7, 37.

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