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CPP: Fachverband Chemische Physik und Polymerphysik
CPP 47: Fluids and Interfaces I
CPP 47.5: Vortrag
Mittwoch, 22. März 2017, 17:30–17:45, ZEU 255
Tuning protein adsorption using multivalent ions — •Madeleine Fries1, Frank Schreiber1, Fajun Zhang1, Alexander Hinderhofer1, Robert Jacobs2, and Maximilian Skoda3 — 1Institut für Angewandte Physik, Universität Tübingen, 72076 Tübingen, Germany — 2Chemistry Research Laboratory, University of Oxford, Oxford, OX1 3TA, United Kingdom — 3Rutherford-Appleton Laboratory, ISIS Facility, Didcot, OX11 0QX, United Kingdom
We studied protein (bovine serum albumin, BSA) adsorption at the solid-liquid interface tuned by trivalent ions (Y3+) using ellipsometry, neutron reflectivity and quartz-crystal microbalance. We find re-entrant behavior of the interface adsorption, which increases upon approaching c* and decreases above c**, where c* and c** are the corresponding critical concentrations marking the region of the re-entrant condensation behavior in the bulk. We thus manage to relate the rich bulk phase behavior, which also features liquid-liquid phase separation and new pathways to crystallization [1] discussed in terms of an ion-activated attractive patch model [2], to the interface adsorption behavior. In addition to the general challenge of connecting bulk and interface behavior, our work has implications for, inter alia, nucleation at interfaces.
[1] Zhang, F.et. al, Physical Review Letters 2008, 101 (14), 148101.
[2] Roosen-Runge, F.; Zhang, F.; Schreiber, F.; Roth, R., Scientific reports 2014, 4, 7016.