Next Article in Journal
Prefabricated and Self-Setting Cement Laminates
Next Article in Special Issue
Drug Release Kinetics of Electrospun PHB Meshes
Previous Article in Journal
Simulation-driven Selection of Electrode Materials Based on Mechanical Performance for Lithium-Ion Battery
Open AccessArticle

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

1
Department of Chemical and Materials Engineering, Faculty of Engineering, University of Alberta, Edmonton, AB T6G 1H9, Canada
2
National Research Council, National Institute for Nanotechnology, Edmonton, AB T6G 2M9, Canada
3
Department of Chemistry, Faculty of Science, University of Alberta, Edmonton, AB T6G 2G2, Canada
*
Author to whom correspondence should be addressed.
Materials 2019, 12(5), 832; https://doi.org/10.3390/ma12050832
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)
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
Show Figures

Graphical abstract

MDPI and ACS Style

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.

Show more citation formats Show less citations formats
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Search more from Scilit
 
Search
Back to TopTop