Assessing the Potential of Folded Globular Polyproteins As Hydrogel Building Blocks

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

doi:10.1021/acs.biomac.6b01877

Assessing the Potential of Folded Globular Polyproteins As Hydrogel Building Blocks

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

Department of Chemistry

University of Leeds

Research output: Contribution to journal › Article › peer-review

38 Citations (SciVal)

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 language	English
Pages (from-to)	636-646
Number of pages	11
Journal	Biomacromolecules
Volume	18
Issue number	2
Early online date	22 Dec 2016
DOIs	https://doi.org/10.1021/acs.biomac.6b01877
Publication status	Published - 13 Feb 2017

Funding

The project was supported by a grant from the Engineering and Physics Sciences Research Council (EP/H049479/1). Dr L. Dougan is supported by a grant from the European Research Council (258259-EXTREME BIOPHYSICS). Experiments at the ISIS Pulsed Neutron were supported by a beam time allocation for SANS 2d from the Science and Technology Facilities Council under Proposal Number RB1520127. The authors thank Diamond Light Source for access to beamline B21 that contributed to the results presented here. This work benefitted from SasView software, originally developed by the DANSE Project under NSF Award DMR-0520547. The authors thank Dr. B. Johnson for the help with adapting the light source to the rheometer, Dr. J. Mattsson and Dr. D. Baker for access and support with the DSC and rheometer, Dr. S.King and Dr. S. Rogers for the support at ISIS.

ASJC Scopus subject areas

Bioengineering
Biomaterials
Polymers and Plastics
Materials Chemistry

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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.",

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Assessing the Potential of Folded Globular Polyproteins As Hydrogel Building Blocks

Abstract

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