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BY 4.0 license Open Access Published by De Gruyter November 26, 2020

Protein Adsorption Hysteresis and Transient States of Fibrinogen and BMP-2 as Model Mechanisms for Proteome-Binding to Implants

H. P Jennissen EMAIL logo , Daniel S. Dohle , Thomas Zmbrink and Michael Meißner

Abstract

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.

Published Online: 2020-11-26
Published in Print: 2020-09-01

© 2020 by Walter de Gruyter Berlin/Boston

This work is licensed under the Creative Commons Attribution 4.0 International License.

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