Bone Morphogenetic Protein 2 (BMP-2) Aggregates Can be Solubilized by Albumin-Investigation of BMP-2 Aggregation by Light Scattering and Electrophoresis

• Published in: Pharmaceutics Vol. 12; no. 12; p. 1143
• Main Authors: Sundermann, Julius, Zagst, Holger, Kuntsche, Judith, Wätzig, Hermann, Bunjes, Heike
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 25.11.2020; MDPI
• Subjects: Aggregates; albumin; BMP-2; Cellulose; E coli; Experiments; Growth factors; Medical equipment; protein aggregation; protein solubilization; protein-protein interactions; Proteins; Signal transduction; United States > US; Germany; protein solubilization; BMP-2; protein aggregation; albumin; protein-protein interactions
• ISSN: 1999-4923; 1999-4923
• DOI: 10.3390/pharmaceutics12121143

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.