Dresden 2006 – scientific programme
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CPP: Chemische Physik und Polymerphysik
CPP 12: POSTER Colloids, Nanoparticles and Self-Organizing Systems
CPP 12.30: Poster
Tuesday, March 28, 2006, 17:00–19:00, P3
Secondary Structure Analysis of Synthetic Spider Silk Proteins by Fourier Transform Infrared Spectroscopy — •Michael Tammer1, Patrick Kölsch1, Ute Slotta2, Thomas Scheibel2, and Friedrich Kremer1 — 1Universität Leipzig, Institut für Experimentelle Physik I, Linnestr. 5, 04103 Leipzig — 2Lehrstuhl für Biotechnologie, Technische Universität München, Lichtenbergstr. 4, 85747 Garching
Silk fibers produced by spiders for their web are extremely thin, lightweight, extendible and very strong. The combination of strength and stretchiness of this material gives a toughness comparable to that of high-tensile steel. Therefore several attempts has been done so far to produce artificial fibres spun from dope solutions composed of genetically modified natural proteins, designer proteins or protein-plastic blends.
In the contribution synthetic silk constructs based on the primary structure elements of the garden spider’s (Araneus diadematus) major dragline silk proteins ADF-3 and ADF-4 are investigated by polarized FTIR spectroscopy. Thin films were prepared by spincoating a protein solution with one or more components forming a silk dope. IR spectra of these films and after solvent treatment with methanol or potassium phosphate were recorded. By analyzing the amide I absorbance band the secondary structure for the proteins of all samples are deduced. The treatment was found to emphasize beta-sheet conformations at the expense of alpha-helix and turn structures.