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.

journal_name

Biomacromolecules

journal_title

Biomacromolecules

authors

Young SL,Gupta M,Hanske C,Fery A,Scheibel T,Tsukruk VV

doi

10.1021/bm300964h

subject

Has Abstract

pub_date

2012-10-08 00:00:00

pages

3189-99

issue

10

eissn

1525-7797

issn

1526-4602

journal_volume

13

pub_type

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