Dresden 2017 – scientific programme

Parts | Days | Selection | Search | Updates | Downloads | Help

CPP: Fachverband Chemische Physik und Polymerphysik

CPP 10: Bioinspired Functional Materials II

CPP 10.11: Talk

Monday, March 20, 2017, 17:45–18:00, ZEU 114

Soft and Tough as well: Morphology and Functional Structure of Spider Silk — A. Markus Anton and •Friedrich Kremer — Institute of Experimental Physics I, University of Leipzig, Germany

Spider dragline silk exhibits remarkable characteristics, such as exceptional biocompatibility or high tensile strength combined with great elasticity. Its mechanical properties are based on a refined architecture on the molecular scale: Proteins with highly repetitive core motifs aggregate into nanometer-sized crystals, rich on alanine in β-sheet secondary structure, surrounded by an amorphous glycine-rich matrix. During spinning the amorphous parts are elongated, which orients both substructures and gives rise to an inherent non-equilibrium state. Thus, external stress is directly transferred to the nanocrystals, while the tendency to contract is counterbalanced by surrounding fiber structure, as demonstrated by FTIR experiments in combination with uniaxial stress [1] or hydrostatic pressure [2].

Until recently it was not possible to artificially recreate this exceptional architecture [3]. We show that wet spinning and post-treatment of a novel biomimetic protein results in fibers with a similar nanostructure and comparable toughness as the natural template [4].

[1] P. Papadopoulos et al., Eur. Phys. J. E 24 (2007) 193–199; [2] A. M. Anton et al., Macromolecules 46 (2013) 4919–4923; [3] A. Heidebrecht et al., Adv. Mater. 27 (2015) 2189–2194; [4] A. M. Anton et al., Manuscript in preparation