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:	Jennissen H. P, Dohle Daniel S., Zmbrink Thomas, Meißner Michael
Formato:	article
Lenguaje:	EN
Publicado:	De Gruyter 2020
Materias:	adsorption and desorption isotherms total internal reflection fluorescence (tirf) tirf-rheometry binding constants hill constants on-rate (k+1) off-rate (k-1) Medicine R
Acceso en línea:	https://doaj.org/article/a619f9761525495eb5e9c5526b9a9284
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spelling	oai:doaj.org-article:a619f9761525495eb5e9c5526b9a92842021-12-05T14:10:42ZProtein Adsorption Hysteresis and Transient States of Fibrinogen and BMP-2 as Model Mechanisms for Proteome-Binding to Implants2364-550410.1515/cdbme-2020-3046https://doaj.org/article/a619f9761525495eb5e9c5526b9a92842020-09-01T00:00:00Zhttps://doi.org/10.1515/cdbme-2020-3046https://doaj.org/toc/2364-5504Protein 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.Jennissen H. PDohle Daniel S.Zmbrink ThomasMeißner MichaelDe Gruyterarticleadsorption and desorption isothermstotal internal reflection fluorescence (tirf)tirf-rheometrybinding constantshill constantson-rate (k+1)off-rate (k-1)MedicineRENCurrent Directions in Biomedical Engineering, Vol 6, Iss 3, Pp 180-184 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	adsorption and desorption isotherms total internal reflection fluorescence (tirf) tirf-rheometry binding constants hill constants on-rate (k+1) off-rate (k-1) Medicine R
spellingShingle	adsorption and desorption isotherms total internal reflection fluorescence (tirf) tirf-rheometry binding constants hill constants on-rate (k+1) off-rate (k-1) Medicine R Jennissen H. P Dohle Daniel S. Zmbrink Thomas Meißner Michael Protein Adsorption Hysteresis and Transient States of Fibrinogen and BMP-2 as Model Mechanisms for Proteome-Binding to Implants
description	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.
format	article
author	Jennissen H. P Dohle Daniel S. Zmbrink Thomas Meißner Michael
author_facet	Jennissen H. P Dohle Daniel S. Zmbrink Thomas Meißner Michael
author_sort	Jennissen H. P
title	Protein Adsorption Hysteresis and Transient States of Fibrinogen and BMP-2 as Model Mechanisms for Proteome-Binding to Implants
title_short	Protein Adsorption Hysteresis and Transient States of Fibrinogen and BMP-2 as Model Mechanisms for Proteome-Binding to Implants
title_full	Protein Adsorption Hysteresis and Transient States of Fibrinogen and BMP-2 as Model Mechanisms for Proteome-Binding to Implants
title_fullStr	Protein Adsorption Hysteresis and Transient States of Fibrinogen and BMP-2 as Model Mechanisms for Proteome-Binding to Implants
title_full_unstemmed	Protein Adsorption Hysteresis and Transient States of Fibrinogen and BMP-2 as Model Mechanisms for Proteome-Binding to Implants
title_sort	protein adsorption hysteresis and transient states of fibrinogen and bmp-2 as model mechanisms for proteome-binding to implants
publisher	De Gruyter
publishDate	2020
url	https://doaj.org/article/a619f9761525495eb5e9c5526b9a9284
work_keys_str_mv	AT jennissenhp proteinadsorptionhysteresisandtransientstatesoffibrinogenandbmp2asmodelmechanismsforproteomebindingtoimplants AT dohledaniels proteinadsorptionhysteresisandtransientstatesoffibrinogenandbmp2asmodelmechanismsforproteomebindingtoimplants AT zmbrinkthomas proteinadsorptionhysteresisandtransientstatesoffibrinogenandbmp2asmodelmechanismsforproteomebindingtoimplants AT meißnermichael proteinadsorptionhysteresisandtransientstatesoffibrinogenandbmp2asmodelmechanismsforproteomebindingtoimplants
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Protein Adsorption Hysteresis and Transient States of Fibrinogen and BMP-2 as Model Mechanisms for Proteome-Binding to Implants

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