Bone morphogenetic protein 2 (BMP-2) aggregates can be solubilized by albumin—investigation of BMP-2 aggregation by light scattering and electrophoresis

Julius Sundermann, Holger Zagst, Judith Kuntsche, Hermann Wätzig, Heike Bunjes*

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Abstrakt

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.

OriginalsprogEngelsk
Artikelnummer1143
TidsskriftPharmaceutics
Vol/bind12
Udgave nummer12
Antal sider20
ISSN1999-4923
DOI
StatusUdgivet - dec. 2020

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