Protein Adsorption Hysteresis and Transient States of Fibrinogen and BMP-2 as Model Mechanisms for Proteome-Binding to Implants
Protein adsorption studies returned to the focus of medical therapeutics, when it was found that up to 2500 non-plasma proteins adsorbed to hip implants during arthroplastic surgery, challenging peri-implant healing models. Questions have re-emerged as to the implications of uncontrolled protein unf...
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| Autores principales: | , , , |
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| Formato: | article |
| Lenguaje: | EN |
| Publicado: |
De Gruyter
2020
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| Materias: | |
| Acceso en línea: | https://doaj.org/article/a619f9761525495eb5e9c5526b9a9284 |
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| Sumario: | Protein adsorption studies returned to the focus of medical therapeutics, when it was found that up to 2500 non-plasma proteins adsorbed to hip implants during arthroplastic surgery, challenging peri-implant healing models. Questions have re-emerged as to the implications of uncontrolled protein unfolding after adsorption. In past studies on the cooperativity of protein binding we discovered protein adsorption hysteresis, a thermodynamically irreversible process. The present precursory study comprises real-time kinetic (TIRF-Rheometry) and equilibrium (125I-tracer ) studies on the hysteretic binding of fibrinogen and rhBMP-2 to titanium and glass surfaces via transient states. Thermodynamic constants (GOn), as well as kinetically derived (K'A ) and hysteresis derived (K'HA ) association constants in the range of 106 to 1012 M-1lead to a consistent picture. |
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