Bone Morphogenetic Protein 2 (BMP-2) Aggregates Can be Solubilized by Albumin-Investigation of BMP-2 Aggregation by Light Scattering and Electrophoresis / by Julius Sundermann, Holger Zagst, Judith Kuntsche, Hermann Wätzig and Heike Bunjes
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..
| Medienart: |
E-Book |
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| Erscheinungsjahr: |
2020 |
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| Erschienen: |
Basel: MDPI ; 2020 Braunschweig: Universitätsbibliothek ; 2020 |
| Ausgabe: |
Online-Ausgabe |
| Enthalten in: |
Pharmaceutics - 2020, 12(12), 1143; https://doi.org/10.3390/pharmaceutics12121143 |
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| Sprache: |
Englisch |
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| Beteiligte Personen: |
Sundermann, Julius [VerfasserIn] |
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| Links: |
nbn-resolving.org [kostenfrei] |
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| BKL: |
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| Umfang: |
1 Online-Ressource |
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| doi: |
10.3390/pharmaceutics12121143 |
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| Weitere IDs: |
urn:nbn:de:gbv:084-2020120414177 |
| funding: |
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| Förderinstitution / Projekttitel: |
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| 520 | |a 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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