Protein corona composition of superparamagnetic iron oxide nanoparticles with various physico-chemical properties and coatings.
Because of their biocompatibility and unique magnetic properties, superparamagnetic iron oxide nanoparticles NPs (SPIONs) are recognized as some of the most prominent agents for theranostic applications. Thus, understanding the interaction of SPIONs with biological systems is important for their safe design and efficient applications. In this study, SPIONs were coated with 2 different polymers: polyvinyl alcohol polymer (PVA) and dextran. The obtained NPs with different surface charges (positive, neutral, and negative) were used as a model study of the effect of surface charges and surface polymer materials on protein adsorption using a magnetic separator. We found that the PVA-coated SPIONs with negative and neutral surface charge adsorbed more serum proteins than the dextran-coated SPIONs, which resulted in higher blood circulation time for PVA-coated NPs than the dextran-coated ones. Highly abundant proteins such as serum albumin, serotransferrin, prothrombin, alpha-fetoprotein, and kininogen-1 were commonly found on both PVA- and dextran-coated SPIONs. By increasing the ionic strength, soft- and hard-corona proteins were observed on 3 types of PVA-SPIONs. However, the tightly bound proteins were observed only on negatively charged PVA-coated SPIONs after the strong protein elution.
Laboratory of Powder Technology, École Polytechnique Fédérale de Lausanne, Lausanne, Switzerland.
Usawadee
U
Sakulkhu
1] Department of Nanotechnology, Faculty of Pharmacy, Tehran University of Medical Sciences, Tehran, Iran [2] Nanotechnology Research Center, Faculty of Pharmacy, Tehran University of Medical Sciences, Tehran, Iran.
Morteza
M
Mahmoudi
Laboratory of Powder Technology, École Polytechnique Fédérale de Lausanne, Lausanne, Switzerland.
Lionel
L
Maurizi
Laboratory of Powder Technology, École Polytechnique Fédérale de Lausanne, Lausanne, Switzerland.
Jatuporn
J
Salaklang
Laboratory of Powder Technology, École Polytechnique Fédérale de Lausanne, Lausanne, Switzerland.
Heinrich
H
Hofmann
D000818:Animals; D001798:Blood Proteins / Q000737:chemistry*; D003287:Contrast Media / Q000737:chemistry*; D005260:Female; D005290:Ferric Compounds / Q000737:chemistry*; D058185:Magnetite Nanoparticles / Q000737:chemistry*; D011108:Polymers / Q000737:chemistry*; D051381:Rats; D011917:Rats, Inbred Lew
D001798:Blood Proteins; D003287:Contrast Media; D005290:Ferric Compounds; D058185:Magnetite Nanoparticles; D011108:Polymers; C000499:ferric oxide