Regensburg 2019 – wissenschaftliches Programm

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CPP: Fachverband Chemische Physik und Polymerphysik

CPP 8: Interfaces and Thin Films (joint session CPP/DY)

CPP 8.4: Vortrag

Montag, 1. April 2019, 15:45–16:00, H14

Enhanced protein adsorption near a phase transition — •Madeleine R. Fries1, Daniel Stopper1, Fajun Zhang1, Robert M. J. Jacobs2, Maximilian W. A. Skoda3, Roland Roth1, and Frank Schreiber11University of Tübingen, Germany — 2University of Oxford, UK — 3ISIS Facility, Didcot, UK

Protein adsorption at the solid-liquid interface is an important phenomenon that often can be observed as a first step in biomedicine. In particular, globular proteins tuned by multivalent ions give rise to a rich phase behavior including reentrant condensation and liquid-liquid phase separation (LLPS) through ion-bridges connecting individual proteins [1, 2]. Multivalent ions can be used not only to modify the bulk behaviour, but also the adsorption behaviour of proteins at the solid-liquid interface [3]. Here, we demonstrate experimentally that protein adsorption at attractive substrates can be enhanced significantly by approaching the LLPS regime through an increase in temperature or protein concentration, pointing towards the ability to control protein adsorption by means of suitably tailoring thermodynamic conditions. This is supported by theoretical calculations treating proteins as limited-valence (patchy) particles. These results could enable better biocompatibility in implants through guided protein-substrate interactions. [1] Zhang et al, PRL (2008); [2] Roosen-Runge et al, Sci. Rep. (2014); [3] Fries et al, PRL (2017)

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