Peptide modification of purified gellan gum

Journal Article


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Abstract


  • Gellan 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.

Publication Date


  • 2015

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.

Scopus Eid


  • 2-s2.0-84928097333

Ro Full-text Url


  • http://ro.uow.edu.au/cgi/viewcontent.cgi?article=2375&context=aiimpapers

Ro Metadata Url


  • http://ro.uow.edu.au/aiimpapers/1373

Has Global Citation Frequency


Number Of Pages


  • 9

Start Page


  • 1106

End Page


  • 1115

Volume


  • 3

Issue


  • 6

Place Of Publication


  • United Kingdom

Abstract


  • Gellan 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.

Publication Date


  • 2015

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.

Scopus Eid


  • 2-s2.0-84928097333

Ro Full-text Url


  • http://ro.uow.edu.au/cgi/viewcontent.cgi?article=2375&context=aiimpapers

Ro Metadata Url


  • http://ro.uow.edu.au/aiimpapers/1373

Has Global Citation Frequency


Number Of Pages


  • 9

Start Page


  • 1106

End Page


  • 1115

Volume


  • 3

Issue


  • 6

Place Of Publication


  • United Kingdom