2 research outputs found

    Cooperative Adsorption of Lipoprotein Phospholipids, Triglycerides, and Cholesteryl Esters Are a Key Factor in Nonspecific Adsorption from Blood Plasma to Antifouling Polymer Surfaces

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    Nonspecific protein adsorption is a central challenge for the use of polymeric materials in biological media. While the quantity of adsorbed protein can be lowered, very few surfaces are protein resistant when exposed to undiluted serum or plasma. The underlying principles of this fouling and the adsorbing proteins remain to be identified. Here, we investigated adsorption from undiluted human blood plasma to three different polymer brushes. Our study showed that the polymer structure does not influence which proteins adsorb. Further, we identified 98 plasma proteins that still foul current ā€œprotein-resistantā€ polymer brushes. Detailed studies into the major adsorbing protein revealed the central role that lipoproteins and low density lipoprotein in particular play in fouling of plasma to polymeric biomaterials. However, although apolipoprotein B100 is found as a major fouling protein in our mass spectrometry screening, studies on individual components of lipoproteins show that it is not apoB100 but a mixture of phospholipids, triglycerides, and cholesteryl esters that plays a major role in lipoprotein adsorption

    Tandem Coordination, Ring-Opening, Hyperbranched Polymerization for the Synthesis of Water-Soluble Coreā€“Shell Unimolecular Transporters

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    A water-soluble molecular transporter with a dendritic coreā€“shell nanostructure has been prepared by a tandem coordination, ring-opening, hyperbranched polymerization process. Consisting of hydrophilic hyperbranched polyglycerol shell grafted from hydrophobic dendritic polyethylene core, the transporter has a molecular weight of 951 kg/mol and a hydrodynamic diameter of 17.5 Ā± 0.9 nm, as determined by static and dynamic light scattering, respectively. Based on evidence from fluorescence spectroscopy, light scattering, and electron microscopy, the coreā€“shell copolymer transports the hydrophobic guests pyrene and Nile red by a unimolecular transport mechanism. Furthermore, it was shown that the coreā€“shell copolymer effectively transports the hydrophobic dye Nile red into living cells under extremely high and biologically relevant dilution conditions, which is in sharp contrast to a small molecule amphiphile. These results suggest potential applicability of such coreā€“shell molecular transporters in the administration of poorly water-soluble drugs
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