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Characterisation of minimalist co-assembled fluorenylmethyloxycarbonyl self-assembling peptide systems for presentation of multiple bioactive peptides

Horgan, Conor C., Rodriguez, Alexandra L., Li, Rui, Bruggeman, Kiara F., Stupka, Nicole, Raynes, Jared K., Day, Li, White, John W., Williams, Richard J. and Nisbet, David R. 2016, Characterisation of minimalist co-assembled fluorenylmethyloxycarbonyl self-assembling peptide systems for presentation of multiple bioactive peptides, Acta biomaterialia, vol. 38, pp. 11-22, doi: 10.1016/j.actbio.2016.04.038.

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Title Characterisation of minimalist co-assembled fluorenylmethyloxycarbonyl self-assembling peptide systems for presentation of multiple bioactive peptides
Author(s) Horgan, Conor C.
Rodriguez, Alexandra L.
Li, Rui
Bruggeman, Kiara F.
Stupka, Nicole
Raynes, Jared K.
Day, Li
White, John W.
Williams, Richard J.
Nisbet, David R.
Journal name Acta biomaterialia
Volume number 38
Start page 11
End page 22
Total pages 12
Publisher Elsevier
Place of publication Amsterdam, The Netherlands
Publication date 2016-07-01
ISSN 1742-7061
1878-7568
Keyword(s) self-assembling peptides
hydrogels
co-assembly
Fmoc
tissue engineering
Science & Technology
Technology
Engineering, Biomedical
Materials Science, Biomaterials
Engineering
Materials Science
NEURAL PROGENITOR CELLS
MOLECULAR-WEIGHT HYDROGELS
REGENERATIVE MEDICINE
MECHANICAL-PROPERTIES
NEURITE OUTGROWTH
HYALURONIC-ACID
BETA-SHEETS
SCAFFOLDS
DIFFERENTIATION
NANOSTRUCTURES
Summary The nanofibrillar structures that underpin self-assembling peptide (SAP) hydrogels offer great potential for the development of finely tuned cellular microenvironments suitable for tissue engineering. However, biofunctionalisation without disruption of the assembly remains a key issue. SAPS present the peptide sequence within their structure, and studies to date have typically focused on including a single biological motif, resulting in chemically and biologically homogenous scaffolds. This limits the utility of these systems, as they cannot effectively mimic the complexity of the multicomponent extracellular matrix (ECM). In this work, we demonstrate the first successful co-assembly of two biologically active SAPs to form a coassembled scaffold of distinct two-component nanofibrils, and demonstrate that this approach is more bioactive than either of the individual systems alone. Here, we use two bioinspired SAPs from two key ECM proteins: Fmoc-FRGDF containing the RGD sequence from fibronectin and Fmoc-DIKVAV containing the IKVAV sequence from laminin. Our results demonstrate that these SAPs are able to co-assemble to form stable hybrid nanofibres containing dual epitopes. Comparison of the co-assembled SAP system to the individual SAP hydrogels and to a mixed system (composed of the two hydrogels mixed together post-assembly) demonstrates its superior stable, transparent, shear-thinning hydrogels at biological pH, ideal characteristics for tissue engineering applications. Importantly, we show that only the coassembled hydrogel is able to induce in vitro multinucleate myotube formation with C2C12 cells. This work illustrates the importance of tissue engineering scaffold functionalisation and the need to develop increasingly advanced multicomponent systems for effective ECM mimicry.

STATEMENT OF SIGNIFICANCE: Successful control of stem cell fate in tissue engineering applications requires the use of sophisticated scaffolds that deliver biological signals to guide growth and differentiation. The complexity of such processes necessitates the presentation of multiple signals in order to effectively mimic the native extracellular matrix (ECM). Here, we establish the use of two biofunctional, minimalist self-assembling peptides (SAPs) to construct the first co-assembled SAP scaffold. Our work characterises this construct, demonstrating that the physical, chemical, and biological properties of the peptides are maintained during the co-assembly process. Importantly, the coassembled system demonstrates superior biological performance relative to the individual SAPs, highlighting the importance of complex ECM mimicry. This work has important implications for future tissue engineering studies.
Language eng
DOI 10.1016/j.actbio.2016.04.038
Field of Research 030199 Analytical Chemistry not elsewhere classified
Socio Economic Objective 970103 Expanding Knowledge in the Chemical Sciences
HERDC Research category C1 Refereed article in a scholarly journal
ERA Research output type C Journal article
Copyright notice ©2016, Acta Materialia
Persistent URL http://hdl.handle.net/10536/DRO/DU:30085353

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