Biomedical Engineering Reference
In-Depth Information
The pro-adhesive properties of galectins have been shown several times. But only few
efforts have been done to elucidate the potential of galectins as coatings for biomaterial
surfaces. In contrast other components of the extracellular matrix are often used. Coatings
with peptides from ECM proteins such as RGD or YIGSR peptide are one of the most
common methods to modify biomaterial surfaces. Also coatings with complete ECM
proteins or specific adhesion proteins have been investigated. Another important molecule
class used in biomaterial research today are growth factors (Chan & Mooney, 2008;
Shekaran & Garcia, 2011; Straley et al., 2010). The functionalisation with glycans or lectins
seems to be underrepresented although their function in natural processes is well known.
Only few studies show the potential of galectins and glycans as biomaterial coatings:
The positive influence of galectins was shown for example as the coating of PLGA scaffolds
with recombinant galectin-1 promotes adhesion and growth of immortal rat chondrocytes.
Therefore this surface is mentioned to have potential as biomaterial in tissue engineering
(Chen et al., 2005). The potential of glycans in biomaterial coatings has also been shown. For
example galactose derivatives immobilised on material surfaces were proven to influence
the growth and function of liver cells positively. But in this study the receptor molecules
and mechanisms of signal transduction were not investigated and binding of an
asialoglycoprotein receptor (and not galectin mediated binding) is assumed (De Bartolo et
al., 2006). Another study shows combined use of immobilised glycans with galectins as it
evidences positive effects of endogenous galectin-1 for adhesion of chondrocytes to a
lactose-modified surface (Marcon et al., 2005). These findings prove the possible use of
glycan and/or galectin modified materials for improved cell adhesion.
Fig. 4. Schematic representation of a possible biomaterial set-up using immobilised glycans
as scaffold for subsequent galectin-mediated protein and cell-adhesion
