Dresden 2006 – scientific programme

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AKB: Biologische Physik

AKB 30: Poster Session I

AKB 30.2: Poster

Monday, March 27, 2006, 15:30–18:00, P1

Structural characterization of recombinant spider silk protein films immobilized to solid surface — •Ezzeldin Metwalli¹, Ute Slotta², Thomas Scheibel², and Christine Papadakis¹ — ¹Physikdepartment E13, Technische Universität München, James-Franck-Str. 1, 85747 Garching, Germany. — ²Chemiedepartment, Lehrstuhl für Biotechnologie, Technische Universität München, Lichtenbergstr. 4, 85747 Garching, Germany.

Mapping the conformational alterations associated with protein adsorption to solid surfaces is important for some applications such as biosensors and chromatographic separations. Recombinant spider silk protein is chosen for our investigation because of excellent mechanical properties, biocompatibility and biodegradability of silk-based materials. A circular dichroism (CD) study [1] on biosynthesized spider silk protein film immobilized to solid surface indicates conformational changes from alfa-helix to beta-sheet structure upon chemical treatment with either methanol or phosphate buffer. Using grazing-incidence small-angle x-ray scattering (GISAXS), the structure of the protein layer before and after the chemical treatments was investigated. This technique provides structural information on a large range of length scales from a few nm up to few microns which helps to characterize the structure of the attached protein layer in relation to the conformational alterations. The 2D GISAXS images of treated versus untreated protein films shows drastic structural variations which is in agreement with the formation of a beta-sheet rich layer upon chemical treatment. [1] D. Huemmerich, U. Slotta, T. Scheibel, Applied Physics A, In press 2005.