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Scaffolds formed via the non-equilibrium supramolecular assembly of the synergistic ECM peptides RGD and PHSRN demonstrate improved cell attachment in 3D

Aye, San-Seint S., Li, Rui, Boyd-Moss, Mitchell, Long, Benjamin, Pavuluri, Sivapriya, Bruggeman, Kiara, Wang, Yi, Barrow, Colin R, Nisbet, David R and Williams, Richard J 2018, Scaffolds formed via the non-equilibrium supramolecular assembly of the synergistic ECM peptides RGD and PHSRN demonstrate improved cell attachment in 3D, Polymers, vol. 10, no. 7, pp. 1-13, doi: 10.3390/polym10070690.

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Title Scaffolds formed via the non-equilibrium supramolecular assembly of the synergistic ECM peptides RGD and PHSRN demonstrate improved cell attachment in 3D
Author(s) Aye, San-Seint S.
Li, Rui
Boyd-Moss, Mitchell
Long, BenjaminORCID iD for Long, Benjamin orcid.org/0000-0002-9442-6824
Pavuluri, Sivapriya
Bruggeman, Kiara
Wang, Yi
Barrow, Colin RORCID iD for Barrow, Colin R orcid.org/0000-0002-2153-7267
Nisbet, David R
Williams, Richard J
Journal name Polymers
Volume number 10
Issue number 7
Article ID 690
Start page 1
End page 13
Total pages 13
Publisher MDPI
Place of publication Basel, Switzerland
Publication date 2018-06-21
ISSN 2073-4360
Keyword(s) self-assembly
hydrogel
peptides
cell adhesion
science & technology
physical sciences
polymer science
Summary 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 α5β1mediated 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-asparticacidphenylalanine- 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.
Language eng
DOI 10.3390/polym10070690
HERDC Research category C1 Refereed article in a scholarly journal
ERA Research output type C Journal article
Copyright notice ©2018, the authors
Free to Read? Yes
Use Rights Creative Commons Attribution licence
Persistent URL http://hdl.handle.net/10536/DRO/DU:30111872

Document type: Journal Article
Collections: School of Life and Environmental Sciences
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Every reasonable effort has been made to ensure that permission has been obtained for items included in DRO. If you believe that your rights have been infringed by this repository, please contact drosupport@deakin.edu.au.