Mechanism of formation of a novel self-assembled protein microsphere system

TL;DRAbstract

The development of proteins into pharmaceutical products is limited by protein denaturation during formulation and processing. The objective of this research was to systematically investigate the effect of changes in the protein solution environment [e.g. pH, temperature, concentration (protein and polymer) and polymer molecular weight] to determine the mechanism of formation of a novel self-assembled protein microsphere system. ^ Soluble complexes were observed in mixtures containing native bovine serum albumin (BSA), poly[ethylene glycol] (PEG) and poly[vinylpyrrolidone] (PVP) at 25°C in acetate buffer (pH 5). Changes in the circular dichroism, fluorescence, surface tension and dynamic light scattering (DLS) data of protein/polymer mixtures occurred at 55°C indicating protein conformational changes. Therefore, microspheres formed by temperature modulated self-assembly and the major mechanism of microsphere formation appears to be similar to simple coacervation involving protein denat

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