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Polymers 2018, 10(7), 690; https://doi.org/10.3390/polym10070690

Scaffolds Formed via the Non-Equilibrium Supramolecular Assembly of the Synergistic ECM Peptides RGD and PHSRN Demonstrate Improved Cell Attachment in 3D

1
Center for Chemistry and Biotechnology, Deakin University, Waurn Ponds, VIC 3217, Australia
2
School of Engineering, RMIT University, Bundoora, VIC 3083, Australia
3
Biofab3D, St. Vincents’ Hospital, Fitzroy, VIC 3000, Australia
4
Faculty of Science and Technology, Federation University, Mt. Helen, VIC 3350, Australia
5
School of Medicine, Deakin University, Waurn Ponds, VIC 3217, Australia
6
Research School of Engineering, Australian National University, Canberra, ACT 0200, Australia
These authors contributed equally to this work.
*
Authors to whom correspondence should be addressed.
Received: 4 May 2018 / Revised: 4 June 2018 / Accepted: 12 June 2018 / Published: 21 June 2018
(This article belongs to the Special Issue Polymer Scaffolds for Biomedical Application)
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Abstract

Self-assembling peptides (SAPs) are a relatively new class of low molecular weight gelators which immobilize their solvent through the spontaneous formation of (fibrillar) nanoarchitectures. As peptides are derived from proteins, these hydrogels are ideal for use as biocompatible scaffolds for regenerative medicine. Importantly, due to the propensity of peptide sequences to act as signals in nature, they are easily functionalized to be cell instructive via the inclusion of bioactive epitopes. In nature, the fibronectin peptide sequence, arginine-glycine-aspartic acid (RGD) synergistically promotes the integrin α5β1 mediated cell adhesion with another epitope, proline-histidine-serine-arginine-asparagine (PHSRN); however most functionalization strategies focus on RGD alone. Here, for the first time, we discuss the biomimetic inclusion of both these sequences within a self-assembled minimalistic peptide hydrogel. Here, based on our work with Fmoc-FRGDF (N-flourenylmethyloxycarbonyl phenylalanine-arginine-glycine-aspartic acid-phenylalanine), we show it is possible to present two epitopes simultaneously via the assembly of the epitopes by the coassembly of two SAPs, and compare this to the effectiveness of the signals in a single peptide; Fmoc-FRGDF: Fmoc-PHSRN (N-flourenylmethyloxycarbonyl-proline-histidine-serine-arginine-asparagine) and Fmoc-FRGDFPHSRN (N-flourenylmethyloxycarbonyl-phenylalanine-arginine-glycine-asparticacid-phenylalanine-proline-histidine-serine-arginine-asparagine). We show both produced self-supporting hydrogel underpinned by entangled nanofibrils, however, the stiffness of coassembled hydrogel was over two orders of magnitude higher than either Fmoc-FRGDF or Fmoc-FRGDFPHSRN alone. In-vitro three-dimensional cell culture of human mammary fibroblasts on the hydrogel mixed peptide showed dramatically improved adhesion, spreading and proliferation over Fmoc-FRGDF. However, the long peptide did not provide effective cell attachment. The results demonstrated the selective synergy effect of PHSRN with RGD is an effective way to augment the robustness and functionality of self-assembled bioscaffolds. View Full-Text
Keywords: self-assembly; hydrogel; peptides; cell adhesion self-assembly; hydrogel; peptides; cell adhesion
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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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Aye, S.-S.S.; Li, R.; Boyd-Moss, M.; Long, B.; Pavuluri, S.; Bruggeman, K.; Wang, Y.; Barrow, C.R.; Nisbet, D.R.; Williams, R.J. Scaffolds Formed via the Non-Equilibrium Supramolecular Assembly of the Synergistic ECM Peptides RGD and PHSRN Demonstrate Improved Cell Attachment in 3D. Polymers 2018, 10, 690.

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