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Title: Peptide modification of purified gellan gum
Authors: Ferris, CJ
Stevens, LR
Gilmore, KJ
Mume, E
Greguric, I
Kirchmajer, DM
Wallace, GG
in het Panhuis, M.
Keywords: Gums
Aspartic acid
Issue Date: 10-Dec-2014
Publisher: Royal Society of Chemistry
Citation: Ferris, C. J., Stevens, L. R., Gilmore, K. J., Mume, E., Greguric, I., Kirchmajer, D. M., Wallace, G. G., in het Panhuis, M. (2015). Peptide modification of purified gellan gum. Journal of Materials Chemistry B, 3(6), 1106-1115. doi:10.1039/C4TB01727G
Abstract: AbstractGellan gum (GG) is an anionic polysaccharide with potential as a biopolymer for additive manufacturing (3D-bioprinting) and tissue engineering. Previous studies have shown GG to be highly cytocompatible, but lacking specific attachment sites required for anchorage-dependent cells. In this work, we modify purified-GG polymer with a short peptide containing the arginine-glycine-aspartic acid (RGD) sequence that is known to enhance integrin-mediated cell attachment. Radiolabelling of the peptide was used in optimisation of the conjugation procedure to achieve an overall efficiency of 40%. The purification of divalent cations from commercial GG samples was found to be critical for successful conjugation. Rheological studies revealed that the peptide coupling did not prevent gelation behaviour. C2C12 cells showed improved attachment on the surface of and encapsulated within RGD-GG hydrogels, differentiating to multinucleated myofibers after 5–7 days. PC12 cells showed minimal interactions with both GG and RGD-GG, with formation of cell clusters and impedance of terminal differentiation and neurite extension. © 2015 Royal Society of Chemistry
ISSN: 2050-7518
Appears in Collections:Journal Articles

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