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Alves da Silva, M; Lenton, S; Hughes, M; Brockwell, DJ; Dougan, L (2017)
Publisher: American Chemical Society
Journal: Biomacromolecules
Languages: English
Types: Article
Subjects: Article

Classified by OpenAIRE into

mesheuropmc: technology, industry, and agriculture, complex mixtures, macromolecular substances
The native states of proteins generally have stable well-defined folded structures endowing these biomolecules with specific functionality and molecular recognition abilities. Here we explore the potential of using folded globular polyproteins as building blocks for hydrogels. Photochemically cross-linked hydrogels were produced from polyproteins containing either five domains of I27 ((I27)5), protein L ((pL)5), or a 1:1 blend of these proteins. SAXS analysis showed that (I27)5 exists as a single rod-like structure, while (pL)5 shows signatures of self-aggregation in solution. SANS measurements showed that both polyprotein hydrogels have a similar nanoscopic structure, with protein L hydrogels being formed from smaller and more compact clusters. The polyprotein hydrogels showed small energy dissipation in a load/unload cycle, which significantly increased when the hydrogels were formed in the unfolded state. This study demonstrates the use of folded proteins as building blocks in hydrogels, and highlights the potential versatility that can be offered in tuning the mechanical, structural, and functional properties of polyproteins.

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Funded by projects

  • EC | EXTREME BIOPHYSICS
  • RCUK | Enabling Tools & Techn...
  • NSF | IMR-MIP DANSE - Distributed...

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