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Utilizing Conformational Changes for Patterning Thin Films of Recombinant Spider Silk Proteins

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School of Materials Science and Engineering, Georgia Institute of Technology, Atlanta, Georgia 30332, United States
Physical Chemistry II, University of Bayreuth, Universitätsstrasse 30, 95447 Bayreuth, Germany
§ Biomaterials, FAN, University of Bayreuth, Universitätsstrasse 30, 95447 Bayreuth, Germany
*Tel.: 404-894-6081; Fax: 404-385-3112; E-mail address: [email protected]
Cite this: Biomacromolecules 2012, 13, 10, 3189–3199
Publication Date (Web):September 4, 2012
https://doi.org/10.1021/bm300964h
Copyright © 2012 American Chemical Society
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Abstract

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Recombinant spider silk proteins mimicking the properties of dragline silk proteins represent a class of materials that hold great potential for future high-performance applications. Here we explore the self-assembly behavior of a recombinantly produced spider silk protein based on the dragline silk of the Araneus diadematus, eADF4 (C16), by selectively patterning its secondary structure using capillary transfer lithography and solvent-assisted microcontact molding. Two conformational transitions were observed, influenced by initial solvent composition: α-helix/random coil conformation to a more densely packed β-sheet conformation (by casting from 1,1,1,3,3,3-hexafluoro-propanol) and moderate initial β-sheet content to higher β-sheet content (casting from formic acid). Furthermore, by using the solvent-assisted microcontact molding technique, we were able to achieve a submicrometer spatial resolution and reveal fine details of morphological and mechanical changes in patterned regions and at interfaces.

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Supporting Information is available that includes additional discussion on the patterning process, the observed tearing observed in the patterned C16 films, the adhesion recorded in these experiments, as well as a note on the stability of the C16 solution. This material is available free of charge via the Internet at http://pubs.acs.org.

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