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  • Transferrin coated nanoparticles: study of the bionano interface in human plasma.

Transferrin coated nanoparticles: study of the bionano interface in human plasma.

PloS one (2012-07-26)
Andrzej S Pitek, David O'Connell, Eugene Mahon, Marco P Monopoli, Francesca Baldelli Bombelli, Kenneth A Dawson
ABSTRACT

It is now well established that the surface of nanoparticles (NPs) in a biological environment is immediately modified by the adsorption of biomolecules with the formation of a protein corona and it is also accepted that the protein corona, rather than the original nanoparticle surface, defines a new biological identity. Consequently, a methodology to effectively study the interaction between nanomaterials and the biological corona encountered within an organism is a key objective in nanoscience for understanding the impact of the nanoparticle-protein interactions on the biological response in vitro and in vivo. Here, we outline an integrated methodology to address the different aspects governing the formation and the function of the protein corona of polystyrene nanoparticles coated with Transferrin by different strategies. Protein-NP complexes are studied both in situ (in human plasma, full corona FC) and after washing (hard corona, HC) in terms of structural properties, composition and second-order interactions with protein microarrays. Human protein microarrays are used to effectively study NP-corona/proteins interactions addressing the growing demand to advance investigations of the extrinsic function of corona complexes. Our data highlight the importance of this methodology as an analysis to be used in advance of the application of engineered NPs in biological environments.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
IgG from human serum, reagent grade, ≥95% (HPLC), buffered aqueous solution
Sigma-Aldrich
MES, low moisture content, ≥99% (titration)
Sigma-Aldrich
Apolipoprotein E, Human Plasma, Very Low-Density Lipoprotein, Native apolipoprotein E from human plasma. A major component of VLDL and IDL. Serves as a major cholesterol carrier. Essential for the normal catabolism of triglyceride-rich lipoprotein constituents.
Sigma-Aldrich
Apolipoprotein A-II, Human Plasma, High-Density Lipoprotein, Native apolipoprotein A-II from human plasma. The second most abundant protein of HDL. Binds to phospholipids during lipoprotein metabolism. Displaces LCAT bound to lipoprotein.
Sigma-Aldrich
Apolipoprotein A-I, Human Plasma, High-Density Lipoprotein, Native apolipoprotein A-I from human plasma. Functions as a cofactor for lecithin-cholesterol acyltransferase. A component of high density lipoprotein.
Sigma-Aldrich
Glycine, ReagentPlus®, ≥99% (HPLC)
Sigma-Aldrich
Apolipoprotein B, Human Plasma, Low-Density Lipoprotein, Native apolipoprotein B from human plasma. It is a dominant protein constituent of LDL and VLDL. Acts as a ligand for LDL receptor, directing clearance of LDL from plasma to the liver.