Enhanced protein adsorption upon bulk phase separation

In all areas related to protein adsorption, from medicine to biotechnology to heterogeneous nucleation, the question about its dominant forces and control arises. In this study, we used ellipsometry and quartz-crystal microbalance with dissipation (QCM-D), as well as density-functional theory (DFT)...

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Main Authors: Fries, MR, Stopper, D, Skoda, MWA, Blum, M, Kertzscher, C, Hinderhofer, A, Zhang, F, Jacobs, RMJ, Roth, R, Schreiber, F
Format: Journal article
Jezik:English
Izdano: Nature Reaserch 2020
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author Fries, MR
Stopper, D
Skoda, MWA
Blum, M
Kertzscher, C
Hinderhofer, A
Zhang, F
Jacobs, RMJ
Roth, R
Schreiber, F
author_facet Fries, MR
Stopper, D
Skoda, MWA
Blum, M
Kertzscher, C
Hinderhofer, A
Zhang, F
Jacobs, RMJ
Roth, R
Schreiber, F
author_sort Fries, MR
collection OXFORD
description In all areas related to protein adsorption, from medicine to biotechnology to heterogeneous nucleation, the question about its dominant forces and control arises. In this study, we used ellipsometry and quartz-crystal microbalance with dissipation (QCM-D), as well as density-functional theory (DFT) to obtain insight into the mechanism behind a wetting transition of a protein solution. We established that using multivalent ions in a net negatively charged globular protein solution (BSA) can either cause simple adsorption on a negatively charged interface, or a (diverging) wetting layer when approaching liquid-liquid phase separation (LLPS) by changing protein concentration (cp) or temperature (T). We observed that the water to protein ratio in the wetting layer is substantially larger compared to simple adsorption. In the corresponding theoretical model, we treated the proteins as limited-valence (patchy) particles and identified a wetting transition for this complex system. This wetting is driven by a bulk instability introduced by metastable LLPS exposed to an ion-activated attractive substrate.
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spelling oxford-uuid:8bff906b-e6ee-4ab0-932e-1e504d5cb0b32022-03-26T22:41:52ZEnhanced protein adsorption upon bulk phase separationJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:8bff906b-e6ee-4ab0-932e-1e504d5cb0b3EnglishSymplectic ElementsNature Reaserch2020Fries, MRStopper, DSkoda, MWABlum, MKertzscher, CHinderhofer, AZhang, FJacobs, RMJRoth, RSchreiber, FIn all areas related to protein adsorption, from medicine to biotechnology to heterogeneous nucleation, the question about its dominant forces and control arises. In this study, we used ellipsometry and quartz-crystal microbalance with dissipation (QCM-D), as well as density-functional theory (DFT) to obtain insight into the mechanism behind a wetting transition of a protein solution. We established that using multivalent ions in a net negatively charged globular protein solution (BSA) can either cause simple adsorption on a negatively charged interface, or a (diverging) wetting layer when approaching liquid-liquid phase separation (LLPS) by changing protein concentration (cp) or temperature (T). We observed that the water to protein ratio in the wetting layer is substantially larger compared to simple adsorption. In the corresponding theoretical model, we treated the proteins as limited-valence (patchy) particles and identified a wetting transition for this complex system. This wetting is driven by a bulk instability introduced by metastable LLPS exposed to an ion-activated attractive substrate.
spellingShingle Fries, MR
Stopper, D
Skoda, MWA
Blum, M
Kertzscher, C
Hinderhofer, A
Zhang, F
Jacobs, RMJ
Roth, R
Schreiber, F
Enhanced protein adsorption upon bulk phase separation
title Enhanced protein adsorption upon bulk phase separation
title_full Enhanced protein adsorption upon bulk phase separation
title_fullStr Enhanced protein adsorption upon bulk phase separation
title_full_unstemmed Enhanced protein adsorption upon bulk phase separation
title_short Enhanced protein adsorption upon bulk phase separation
title_sort enhanced protein adsorption upon bulk phase separation
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AT stopperd enhancedproteinadsorptionuponbulkphaseseparation
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