Journal
PHARMACEUTICS
Volume 12, Issue 12, Pages -Publisher
MDPI
DOI: 10.3390/pharmaceutics12121143
Keywords
BMP-2; albumin; protein aggregation; protein-protein interactions; protein solubilization
Categories
Funding
- Deutsche Forschungsgemeinschaft [FOR 2180]
- Technische Universitat Braunschweig
- Leibniz Universitat Hannover by the Ministry of Science and Culture (MWK) of Lower Saxony, Germany
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Bone morphogenetic protein 2 (BMP-2) has a high tendency to aggregate at physiological pH and physiological ionic strength, which can complicate the development of growth factor delivery systems. The aggregation behavior in differently concentrated BMP-2 solutions was investigated using dynamic and static light scattering. It was found that at higher concentrations larger aggregates are formed, whose size decreases again with increasing dilution. A solubilizing effect and therefore less aggregation was observed upon the addition of albumin. Imaged capillary isoelectric focusing and the simulation of the surface charges of BMP-2 were used to find a possible explanation for the unusually low solubility of BMP-2 at physiological pH. In addition to hydrophobic interactions, attractive electrostatic interactions might be decisive in the aggregation of BMP-2 due to the particular distribution of surface charges. These results help to better understand the solubility behavior of BMP-2 and thus support future pharmaceutical research and the development of new strategies for the augmentation of bone healing.
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