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Florian Evers: „Proteins at interfaces - X-ray and neutron scattering studies”
Fakultät Physik & DELTA TU Dortmund

Protein adsorption on solid and liquid surfaces has implications in such diverse fields as drug delivery, biocompatibility of implants, biofouling, food chemistry, and biosensors. The interfacial affinity of proteins is ruled by a complex interplay between protein-protein and protein-surface interactions in an aqueous environment. In order to analyze the interfacial structure and composition of adsorbed protein films, neutron and X-ray reflectometry serve as powerful tools.

So far, strategies to prevent protein adsorption have mainly focused on the role of surface chemistry and protein structure, whereas the influence of solvent composition on protein adsorption has often been neglected. Here, comprehensive studies on the effects of ionic and non-ionic cosolvents on protein adsorption will be presented [1,2]. It will be shown that both protein-stabilizing and protein-destabilizing cosolvents can be used to control the degree of protein adsorption.

Furthermore, the interaction of insulin with polyelectrolyte brushes will be discussed [3]. In contrast to other model proteins, insulin is an aggregation-prone peptide and can form amyloid fibrils. Interestingly, the amyloidogenic propensity of insulin can be suppressed by a poly(acrylic acid) brush, qualifying PAA brushes as a potential biocompatible coating for insulin.

Finally, investigations on lipid-peptide interactions and amyloid formation at interfaces will be discussed briefly [4].


  1. Evers et al., JPC B 113 (2009) 8462.
  2. Hüsecken et al., Langmuir 26 (2010) 13429.
  3. Evers et al., PCCP 12 (2010) 4375.
  4. Evers et al., JACS 131 (2009) 9516.