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Enzymatic catalysed synthesis and gelation of ionic peptides for 3D cell culture applications.

Published online by Cambridge University Press:  22 August 2012

Jean-Baptiste Guilbaud
Affiliation:
The University of Manchester, School of Materials, Manchester, M13 9PL, UK
Laura Szkolar
Affiliation:
The University of Manchester, School of Materials, Manchester, M13 9PL, UK
Aline F. Miller
Affiliation:
The University of Manchester, School of Chemical Engineering and Analytical Sciences and Manchester Interdisciplinary Biocentre, Manchester, M13 9PL, UK
Alberto Saiani
Affiliation:
The University of Manchester, School of Materials, Manchester, M13 9PL, UK
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Abstract

The enzymatic catalyzed synthesis and gelation of an ionic peptide and its use to create hydrogels for 3D cell culture is discussed. Time resolved small angle scattering in conjunction with imaging technique allowed the structural changes occurring through this enzymatic reaction to be assessed. In turn, the structural information about the fibrillar network and its local density proved key in facilitating the understanding of the relationships between self-assembly behavior, local nanostructure and final physical properties of the materials. The understanding of the gelation process of these materials allowed the design of a simple and efficient methodology to prepare gels for cell culture. Tetrapeptide/enzyme solution containing cells could be injected into cell culture plate with subsequent gelation of the materials leading to encapsulation of the cells into a 3D network. This system was evaluated for the 3D cell culture of human dermal fibroblasts (HDF). Microscopy showed that cells were uniformly distributed within the gel matrix. Cell counting and live/dead staining showed proliferation of HDF with limited cell death over 10 days.

Type
Articles
Copyright
Copyright © Materials Research Society 2012

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References

REFERENCES

1. Haines, L.A., Rajagopal, K., Ozbas, B., Salick, D.A., Pochan, D.J. and Schneider, J.P., J. Am. Chem. Soc. 127 (48), 1702517029 (2005).Google Scholar
2. Tang, C., Smith, A.M., Collins, R.F., Ulijn, R.V. and Saiani, A., Langmuir 25 (16), 94479453 (2009).Google Scholar
3. Ozbas, B., Kretsinger, J., Rajagopal, K., Schneider, J.P. and Pochan, D.J., Macromolecules 37 (19), 73317337 (2004).Google Scholar
4. Guilbaud, J.-B., Vey, E., Boothroyd, S., Smith, A.M., Ulijn, R.V., Saiani, A. and Miller, A.F., Langmuir 26 (13), 1129711303.Google Scholar
5. Saiani, A., Mohammed, A., Frielinghaus, H., Collins, R., Hodson, N., Kielty, C.M., Sherratt, M.J. and Miller, A.F., Soft Matter 5 (1), 193202 (2009).Google Scholar
6. Mohammed, A., Miller, A.F. and Saiani, A., Macromol. Symp. 251, 8895 (2007).Google Scholar
7. Yan, H., Frielinghaus, H., Nykanen, A., Ruokolainen, J., Saiani, A. and Miller, A. F., Soft Matter 4 (6), 13131325 (2008).Google Scholar
8. Yan, H., Saiani, A., Gough, J.E. and Miller, A.F., Biomacromolecules 7 (10), 27762782 (2006).Google Scholar
9. Bowerman, C.J., Ryan, D.M., Nissan, D.A. and Nilsson, B.L., Molecular BioSystems 5 (9), 10581069 (2009).Google Scholar
10. Caplan, M.R., Schwartzfarb, E.M., Zhang, S.G., Kamm, R.D. and Lauffenburger, D.A., Biomaterials 23 (1), 219227 (2002).Google Scholar
11. Guilbaud, J.-B. and Saiani, A., Chemical Society Reviews 40 (3), 12001210 (2011).Google Scholar
12. Hammouda, B., Journal of Applied Crystallography 43, 716719 (2010).Google Scholar
13. Pupa, S.M., Menard, S., Forti, S. and Tagliabue, E., Journal of Cellular Physiology 192 (3), 259267 (2002).Google Scholar