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Materials 2019, 12(5), 832;

Charge and Peptide Concentration as Determinants of the Hydrogel Internal Aqueous Environment

Department of Chemical and Materials Engineering, Faculty of Engineering, University of Alberta, Edmonton, AB T6G 1H9, Canada
National Research Council, National Institute for Nanotechnology, Edmonton, AB T6G 2M9, Canada
Department of Chemistry, Faculty of Science, University of Alberta, Edmonton, AB T6G 2G2, Canada
Author to whom correspondence should be addressed.
Received: 5 February 2019 / Revised: 6 March 2019 / Accepted: 8 March 2019 / Published: 12 March 2019
(This article belongs to the Special Issue Biocompatible and Biodegradable 3D Scaffolds)
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Self-assembling peptides are a promising class of biomaterials with desirable biocompatibility and versatility. In particular, the oligopeptide (RADA)4, consisting of arginine (R), alanine (A), and aspartic acid (D), self-assembles into nanofibers that develop into a three-dimensional hydrogel of up to 99.5% (w/v) water; yet, the organization of water within the hydrogel matrix is poorly understood. Importantly, peptide concentration and polarity are hypothesized to control the internal water structure. Using variable temperature deuterium solid-state nuclear magnetic resonance (2H NMR) spectroscopy, we measured the amount of bound water in (RADA)4-based hydrogels, quantified as the non-frozen water content. To investigate how peptide polarity affects water structure, five lysine (K) moieties were appended to (RADA)4 to generate (RADA)4K5. Hydrogels at 1 and 5% total peptide concentration were prepared from a 75:25 (w/w) blend of (RADA)4:(RADA)4K5 and similarly analyzed by 2H NMR. Interestingly, at 5% peptide concentration, there was lower mobile water content in the lysinated versus the pristine (RADA)4 hydrogel. Regardless of the presence of lysine, the 5% peptide concentration had higher non-frozen water content at temperatures as low as 217 ± 1.0 K, suggesting that bound water increases with peptide concentration. The bound water, though non-frozen, may be strongly bound to the charged lysine moiety to appear as immobilized water. Further understanding of the factors controlling water structure within hydrogels is important for tuning the transport properties of bioactive solutes in the hydrogel matrix when designing for biomedical applications. View Full-Text
Keywords: self-assembly; peptide chemistry; (RADA)4; vicinal water structure; nanofiber; hydrogel self-assembly; peptide chemistry; (RADA)4; vicinal water structure; nanofiber; hydrogel

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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

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Elgersma, S.V.; Ha, M.; Yang, J.-L.J.; Michaelis, V.K.; Unsworth, L.D. Charge and Peptide Concentration as Determinants of the Hydrogel Internal Aqueous Environment. Materials 2019, 12, 832.

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