Interfacial crystallization and supramolecular self-assembly of spider silk inspired protein at the water-air interface

Pezhman Mohammadi*, Fabian Zemke, Wolfgang Wagermaier, Markus B. Linder

*Corresponding author for this work

Research output: Contribution to journalArticleScientificpeer-review

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Abstract

Macromolecular assembly into complex morphologies and architectural shapes is an area of fundamental research and technological innovation. In this work, we investigate the self-assembly process of recombinantly produced protein inspired by spider silk (spidroin). To elucidate the first steps of the assembly process, we examined highly concentrated and viscous pendant droplets of this protein in air. We show how the protein self-assembles and crystallizes at the water-air interface into a relatively thick and highly elastic skin. Using time-resolved in situ synchrotron x-ray scattering measurements during the drying process, we showed that the skin evolved to contain a high β-sheet amount over time. We also found that β-sheet formation strongly depended on protein concentration and relative humidity. These had a strong influence not only on the amount, but also on the ordering of these structures during the β-sheet formation process. We also showed how the skin around pendant droplets can serve as a reservoir for attaining liquid-liquid phase separation and coacervation from the dilute protein solution. Essentially, this study shows a new assembly route which could be optimized for the synthesis of new materials from a dilute protein solution and determine the properties of the final products.

Original languageEnglish
Article number4239
Number of pages13
JournalMaterials
Volume14
Issue number15
Early online date29 Jul 2021
DOIs
Publication statusPublished - 1 Aug 2021
MoE publication typeA1 Journal article-refereed

Keywords

  • Coacervate
  • Conformational conversion
  • Liquid-liquid phase separation
  • Skin formation
  • Spider silk
  • X-ray diffraction
  • β-sheet

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