Collagen is the main component of connective tissue, providing structural stability in skin and bones and modulates a variety of cellular activities. The development of collagen based biomaterials as scaffolds for cell growth has gained great interest in the last few years [1]. In order to generate “smart” biomaterials, that are biomaterials capable to generate diverse stimuli such as cell adhesion, proliferation or differentiation, the scaffold should contain the biomolecules responsible for such effects, or at least the minimal molecular structure that elicits this effect. Those molecular entities are mainly peptides or carbohydrates. The decoration of biocompatible scaffolds with peptides has been widely reported in the literature, whereas the glycosylation is much more rare [2,3].
In this work we describe an easy protocol for collagen glycosylation at the lysine residues, exploiting a classical reductive amination protocol. Preliminary biological assays and structural analysis will be presented.
[1] A M Ferreira, P Gentile, V Chiono, G Ciardelli Acta Biomaterialia 2012, 8, 3191–3200.
[2] L. Cipolla, L. Russo, F Taraballi, C. Lupo, D Bini, L Gabrielli, A Capitoli, F Nicotra. Smart biomaterials: the contribution of glycoscience in Specialist Periodical Reports, SPR Carbohydrate Chemistry, 2012, Vol. 38, Chapter 17, 416-445. ISBN: 9781849734394.
[3] L Cipolla, L Russo, N Shaikh, F Nicotra Materials biofunctionalization for tissue re generation in POLYMERIC BIOMATERIALS III ED, Vol. I Polymers as Biomaterials CRC Press, 2013 ISBN 9781420094725.
Acknowledgments:
We gratefully acknowledge Fondazione Cariplo, grant n° 2011-0270 and MIUR, under project PRIN 2010/L9SH3K. for financial support.
