Berlin 2018 – wissenschaftliches Programm
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CPP: Fachverband Chemische Physik und Polymerphysik
CPP 4: Complex Fluids and Colloids I (joint session CPP/DY)
CPP 4.6: Vortrag
Montag, 12. März 2018, 10:45–11:00, C 264
Behavior under shear of solutions of bovine serum albumin and trivalent cations — •Stefano Da Vela1, Miriam Siebenbürger2, Alessio Zaccone3, Fajun Zhang1, Matthias Ballauff2,4, and Frank Schreiber1 — 1Institut für Angewandte Physik, University of Tübingen, Tübingen, Germany — 2Helmholtz Zentrum für Materialien und Energie, Berlin, Germany — 3Dept. of Chemical Engineering and Biotechnology, University of Cambridge, Cambridge, UK — 4Department of Physics, Humboldt-University, Berlin, Germany
Trivalent cations such as Y(III) and La(III) have been shown to induce a rich phase behavior in aqueous solutions of acidic proteins. Thanks to the specific association of the cations with the negatively charged groups on the protein surface, these systems feature directional, patchy interactions. Here we show how shear stress can trigger aggregation in solutions of the acidic protein bovine serum albumin (BSA) in the presence of La(III). The trivalent cation renders the system unstable at high shear rates and the solutions become turbid. Simultaneously a low wavevector upturn develops in small-angle neutron scattering profiles. We discuss the findings in relations to the available theoretical models. As directionality and anisotropy of the interaction are common in proteins, a better understanding of the role of patchiness for shear-induced aggregation is important for many biotechnological operations such as filtration, stirring, filling of containers, and pumping.