1. ABOUT THE DATASET -------------------- Title:Tuning Protein Hydrogel Mechanics through Modulation of Nanoscale Unfolding and Entanglement in Postgelation Relaxation Creator(s): Matt D. G. Hughes [1], Sophie Cussons [2,3], Najet Mahmoudi[4], David J. Brockwell[2,3], and Lorna Dougan[1,2] Organisation(s): [1] School of Physics and Astronomy, Faculty of Engineering and Physical Sciences, University of Leeds, Leeds, LS2 9JT, UK [2] Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, LS2 9JT, UK [3] School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, UK [4] ISIS Neutron and Muon Spallation Source, STFC Rutherford Appleton Laboratory, Oxfordshire, OX11 0QX, UK Rights-holder(s): University of Leeds, American Chemistry Society Publication Year:2022 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. Cite as: Matt D. G. Hughes, Sophie Cussons, Najet Mahmoudi, David J. Brockwell, and Lorna Dougan (2022): Tuning Protein Hydrogel Mechanics through Modulation of Nanoscale Unfolding and Entanglement in Postgelation Relaxation. [Dataset]. https://doi.org/10.5518/1174 Related publication: Matt D. G. Hughes et al. (2022): Tuning Protein Hydrogel Mechanics through Modulation of Nanoscale Unfolding and Entanglement in Postgelation Relaxation. ACS Nano (2022) (In press) https://doi.org/10.1021/acsnano.2c02369 Contact: Lorna Dougan, L.dougan@leeds.ac.uk 2. TERMS OF USE --------------- Copyright 2022 University of Leeds, American Chemistry Society. This dataset is licensed under a Creative Commons Attribution 4.0 International Licence: https://creativecommons.org/licenses/by/4.0/.] 3. PROJECT AND FUNDING INFORMATION ---------------------------------- Funding organisations: EPSRC, BBSRC, White Rose Grant no.:(EP/P02288X/1). 4. CONTENTS ----------- File listing - Zip folder containing all rheology data spread across 2 excel spreadsheets for U-MBP and MB-MBP. - Zip folder containing all DSC data, for U- and MB-MBP in different [Urea] and relevant buffer scans, a further readme is included here. - Zip folder containg reduced SAXS data for two repeats of U-MBP and MB-MBP hydrogels in differeing [urea].