McAvan, BS, Khuphe, M orcid.org/0000-0002-6289-8675 and Thornton, PD orcid.org/0000-0003-3876-1617 (2017) Polymer Hydrogels for Glutathione-Mediated Protein Release. European Polymer Journal, 87. pp. 468-477. ISSN 0014-3057
Abstract
The use of amine-terminated poly(ethylene glycol) star polymers as macroinitiators for the N-carboxyanhydride ring-opening polymerisation of S-tert-butylmercapto-L-cysteine N-carboxahydride is described to yield amphiphilic copolymers that are capable of forming discrete particles in aqueous solution. Poly(amino acid) deprotection liberates the pendant thiol groups that can then form covalent disulfide crosslinks with adjacent thiol groups and yield a crosslinked polymer that is capable of hydrogel formation. The model protein albumin–fluorescein isothiocyanate conjugate was encapsulated within the hydrogels produced, prior to its release upon hydrogel interaction with the reducing agent glutathione. Consequently, the stimuli-responsive polymers formed hold great promise as biomaterials capable of releasing a protein molecular cargo upon interaction with glutathione.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | (c) 2016, Elsevier. This is an author produced version of a paper published in European Polymer Journal. Uploaded in accordance with the publisher's self-archiving policy. |
Keywords: | Stimuli-responsive polymers; Glutathione-mediated degradation; Protein delivery; Polymeric biomaterials |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Engineering & Physical Sciences (Leeds) > School of Chemistry (Leeds) > Colour Science (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 23 Sep 2016 14:01 |
Last Modified: | 11 Jan 2023 11:52 |
Published Version: | https://doi.org/10.1016/j.eurpolymj.2016.09.032 |
Status: | Published |
Publisher: | Elsevier |
Identification Number: | 10.1016/j.eurpolymj.2016.09.032 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:105113 |