title: Utilizing conformational changes for patterning thin films of recombinant spider silk proteins.
abstract: 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.
authors.affiliation: School of Materials Science and Engineering, Georgia Institute of Technology, Atlanta, GA, USA.
authors.forename: Seth L
authors.initials: SL
authors.lastname: Young
authors.forename: Maneesh
authors.initials: M
authors.lastname: Gupta
authors.forename: Christoph
authors.initials: C
authors.lastname: Hanske
authors.forename: Andreas
authors.initials: A
authors.lastname: Fery
authors.forename: Thomas
authors.initials: T
authors.lastname: Scheibel
authors.forename: Vladimir V
authors.initials: VV
authors.lastname: Tsukruk
mesh_terms: D000818:Animals; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry; D047011:Silk / Q000737:chemistry*; D013112:Spiders / Q000737:chemistry*
chemical_list: D011994:Recombinant Proteins; D047011:Silk