Assessing the Potential of Folded Globular Polyproteins As Hydrogel Building Blocks

Marcelo A. Da Silva, Samuel Lenton, Matthew Hughes, David J. Brockwell, Lorna Dougan

Research output: Contribution to journalArticlepeer-review

12 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)636-646
Number of pages11
JournalBiomacromolecules
Volume18
Issue number2
Early online date22 Dec 2016
DOIs
Publication statusPublished - 13 Feb 2017

ASJC Scopus subject areas

  • Bioengineering
  • Biomaterials
  • Polymers and Plastics
  • Materials Chemistry

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