Letter abstract
Nature Materials 4, 772 - 775 (2005)
Published online: 25 September 2005 | doi:10.1038/nmat1493
Subject Categories: Polymers | Biological materials | Characterisation and analytical techniques | Mechanical properties
Differential polymerization of the two main protein components of dragline silk during fibre spinning
Alexander Sponner, Eberhard Unger, Frank Grosse & Klaus Weisshart
Spider silks are some of the strongest materials found in nature1, 2. Achieving the high tensile strength and elasticity of the dragline of orb-weaving spiders, such as Nephila clavipes3, 4, 5, is a principal goal in biomimetics research. The dragline has a composite nature and is predominantly made up by two proteins, the major ampullate spidroins 1 and 2 (refs 3,6,7), which can be considered natural block copolymers8. On the basis of their molecular structures both spidroins are thought to contribute, in different ways, to the mechanical properties of dragline silk9. The spinning process itself is also considered important for determining the observed features by shaping the hierarchical structure of the fibre10, 11. Here we study the heterogeneous distribution of proteins along the radial axis of the fibre. This heterogeneity is generated during the conversion of the liquid spinning dope into solid fibre. Whereas spidroin 1 is distributed almost uniformly within the fibre core, spidroin 2 is missing in the periphery and is tightly packed in certain core areas. Our findings suggest that the role of spidroin 2 in the spinning process could be to facilitate the formation of fibrils and contribute directly to the elasticity of the silk.
- Institute for Molecular Biotechnology, Beutenbergstrasse 11, 07745 Jena, Federal Republic of Germany
Correspondence to: Alexander Sponner Present address: University of Oxford, Department of Zoology, South Parks Road, Oxford OX1 3PS, UK
Correspondence to: Klaus Weisshart Present address: Carl Zeiss Jena GmbH, Carl-Zeiss-Promenade 10, 07745 Jena, Germany
Correspondence to: Klaus Weisshart e-mail: weisshart@zeiss.de
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