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BP: Fachverband Biologische Physik
BP 14: Posters: Protein Structure and dynamics
BP 14.14: Poster
Tuesday, April 1, 2014, 09:30–12:30, P1
Adsorption kinetics and structure of hydrophobins at interfaces — •Jonas Raphael Heppe1, Hendrik Hähl1, Philipp Hudalla2, Ludger Santen2, and Karin Jacobs1 — 1Saarland University, Experimental Physics, D-66041 Saarbrücken — 2Saarland University, Theoretical Physics, D-66041 Saarbrücken
Protein adsorption to interfaces is a common, but complex process with many applications. Besides the attachment to the solid/liquid interface, the adsorption to the interface between water and other liquids or air is of major technological interest. Amphiphilic proteins stabilize this interface and hence serve as emulsifying or foaming agent. To control the processes, a deeper understanding of the competitive processes and interactions leading to the final adsorbate is necessary.
Hydrophobins (HFB) are a class of proteins that may serve as ideal model candidates. Produced by filamentous fungi, they are conformationally stable, highly surface active, and form ordered monolayers at the water surface [1]. We studied the adsorption of HFB wild types and specifically designed mutants featuring different geometry or charge.
To access the adsorption kinetics, we used ellipsometry to record in situ the adsorbed amount at the air/water interface and on solid substrates varying the conditions of surface and solution. Moreover, we analyzed the resulting structure of the adsorbates by applying XRR.
Our results reveal differences in the adsorption kinetics depending on the electrical and steric properties of the proteins as well as the ambient parameters. The experiments are accompanied by theoretical modeling. [1] S. Varjonen et al., Soft Matter 7 (2011) 2402