Research Data Leeds Repository

Citation

Hughes, Matt D. G. and Cussons, Sophie and Mahmoudi, Najet and Brockwell, David J. (2022) Tuning Protein Hydrogel Mechanics through Modulation of Nanoscale Unfolding and Entanglement in Postgelation Relaxation. University of Leeds. [Dataset] https://doi.org/10.5518/1174

Dataset description

Globular folded proteins are versatile nanoscale building blocks to create biomaterials with mechanical robustness and inherent biological functionality due to their specific and well-defined folded structures.

Modulating the nanoscale unfolding of protein building blocks during network formation (in situ protein unfolding) provides potent opportunities to control the protein network structure and mechanics.

Here, we control protein unfolding during the formation of hydrogels constructed from chemically cross-linked maltose binding protein using ligand binding and the addition of cosolutes to modulate protein kinetic and thermodynamic stability.

Bulk shear rheology characterizes the storage moduli of the bound and unbound protein hydrogels and reveals a correlation between network rigidity, characterized as an increase in the storage modulus, and protein thermodynamic stability.

Furthermore, analysis of the network relaxation behavior identifies a crossover from an unfolding dominated regime to an entanglement dominated regime.

Control of in situ protein unfolding and entanglement provides an important route to finely tune the architecture, mechanics, and dynamic relaxation of protein hydrogels.

Such predictive control will be advantageous for future smart biomaterials for applications which require responsive and dynamic modulation of mechanical properties and biological function.

Divisions:	Faculty of Engineering and Physical Sciences > Centre for Molecular Nanoscience (CMNS)
Related resources:	Location Type https://doi.org/10.1021/acsnano.2c02369 Publication https://eprints.whiterose.ac.uk/189307/ Publication
License:	Creative Commons Attribution 4.0 International (CC BY 4.0)
Date deposited:	21 Jun 2022 15:03
URI:	https://archive.researchdata.leeds.ac.uk/id/eprint/988
Additional details Additional details Creators or authors: Creators ORCID Other ID Email Primary affiliation Primary affiliation ID Primary affiliation ID type Secondary affiliation Secondary affiliation ID Secondary affiliation ID type Hughes, Matt D. G. https://orcid.org/0000-0001-5838-7939 University of Leeds https://ror.org/024mrxd33 ror Cussons, Sophie https://orcid.org/0000-0002-9318-3859 University of Leeds https://ror.org/024mrxd33 ror Mahmoudi, Najet https://orcid.org/0000-0003-4936-6911 Rutherford Appleton Laboratory https://ror.org/03gq8fr08 ror Brockwell, David J. https://orcid.org/0000-0002-0802-5937 University of Leeds https://ror.org/024mrxd33 ror Type of data: Dataset Research funders: EPSRC Grant numbers: EP/P02288X/1 Publication date: 2022 Resource language: English Metadata language: English Publisher: University of Leeds Contact email: l.dougan@leeds.ac.uk Last Modified: 24 Jul 2024 14:16

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