Summary: The solubilization and encapsulation of the weakly soluble protein hemoglobin was investigated at the nanoscale using self‐assembly with the branched polymer polyethyleneimine (PEI), the lipid glycerol monooleate (GMO), and two amphiphilic poly(ethylenglycol) monooleate derivatives with molecular weights 2100 g/mol (MO‐PEG1) and 860 g/mol (MO‐PEG2). The created self‐assembly nanovehicles were analyzed by quasi‐elastic light scattering (QELS) in order to determine their sizes as well as by circular dichroism in order to characterize the protein presence in the nanoobjects. The cationic polymer PEI formed mixed nano‐objects with the protein hemoglobin. The polymer conformation in the nanovehicle was established to be sensitive to dilution, a property that can be essential for the protein release upon administration. The amphiphile MO‐PEG1 was a co‐surfactant in the dispersion of monoglyceride lipid nanoobjects needed for the hemoglobin encapsulation. The amphiphile MO‐PEG2 formed small micelles in the absence of a lipid. The nanoobjects dispersions were studied for their stability on storage and reproducibility.
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