Berlin 2018 – wissenschaftliches Programm
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CPP: Fachverband Chemische Physik und Polymerphysik
CPP 14: Interfaces and Thin Films I
CPP 14.5: Vortrag
Montag, 12. März 2018, 16:00–16:15, C 264
Multivalent-Ion-Activated Protein Adsorption Reflecting Bulk Reentrant Behavior — •Madeleine Fries1, Daniel Stopper2, Michal K. Braun1, Alexander Hinderhofer1, Fajun Zhang1, Robert M. J. Jacobs3, Maximilian W. A. Skoda4, Hendrik Hansen-Goos2, Roland Roth2, and Frank Schreiber1 — 1Institute for Applied Physics, University of Tübingen — 2Institute for Theoretical Physics, University of Tübingen — 3Department for Chemistry, Chemistry Research Laboratory, University of Oxford, UK — 4Rutherford-Appleton Laboratory, ISIS Facility, Didcot, UK
Protein adsorption at the solid-liquid interface is an important phenomenon that often can be observed as a first step in biological processes. Despite its inherent importance, still relatively little is known about the underlying microscopic mechanisms. Here, using multivalent ions, we demonstrate the control of the interactions and the corresponding adsorption of net-negatively charged proteins (BSA) at an interface (SiO2) by ellipsometry. We show that the reentrant condensation observed within the rich bulk [1] phase behavior of the system featuring a nonmonotonic dependence of the second virial coefficient on salt concentration cs is reflected in an intriguing way in the protein adsorption d(cs) at the interface. Our findings are successfully described and understood by a model of ion-activated patchy interactions within the framework of classical density functional theory. In addition to the general challenge of connecting bulk and interface behavior, our work has implications for, inter alia, nucleation at interfaces [2].
[1] Fries et al, PRL (2017); [2] Zhang et al, PRL (2008).