Dresden 2020 – scientific programme
The DPG Spring Meeting in Dresden had to be cancelled! Read more ...
Parts | Days | Selection | Search | Updates | Downloads | Help
BP: Fachverband Biologische Physik
BP 17: Poster V
BP 17.6: Poster
Tuesday, March 17, 2020, 14:00–16:00, P2/1OG
Analysis of protein secondary structure in silkworm and spider silk fibroins using Raman spectroscopy — •Emilia Pozarowska1, Tomasz Runka2, and Jan Ingo Flege1 — 1BTU Cottbus - Senftenberg, Germany — 2Poznan University of Technology, Poland
Spider silks carry outstanding mechanical properties, such as the combination of high strength and large extensibility. The aim of this work is to investigate the protein secondary structure, in particular β - sheets, occurring in silkworm and spider silk fibers from different species, by Raman spectroscopy. The analysis of the Raman spectra provides information about characteristic conformations, such as amide I, III and protein secondary structure. A Steatoda grossa spider silk was compared with a silk of the Bombyx mori silkworm. The former shows smaller amount of β - sheets and more random coil and/or α - helix, suggesting better elastic properties. Furthermore, the analysis of dragline silks of 16 different spider species was performed resulting in specific Raman fingerprints corresponding to the silk structure and the sequence of amino acids within. Dragline silks of P. alticeps and S. grossa exhibit a larger contribution of proline and carbonyl (C=O) groups compared to other species. Data of polarized Raman spectroscopy confirmed the parallel alignment of the molecular chains to the fiber axis for all spider silks. Stress-strain curve measurements of one selected spider silk, tubiliform silk of S. grossa, revealed very good mechanical properties, i.e. a maximal strain of approximately 12.2% and final tensile stress at break of 1575 MPa.