Myriad biological processes are governed by chemical
reactions that occur on cell surfaces. In the first
part of this work, a novel approach to direct
biological processes that occur at the surface of
artificial materials is described. A multi-faceted
strategy has been developed to construct 'interfacial
biomaterials' that mediate specific biological
processes via increased cellular adhesion to
medically-relevant materials. A phage display
selection strategy was developed to identify peptides
that show increased affinity for natural and
artificial substrates. In the second part, the
molecular basis of protein-carbohydrate binding is
considered. Ligands displaying lactose epitopes were
constructed to investigate their aggregative
properties towards full-length and truncated
galectin-3. ITC studies with full-length protein
shows a greater than two-fold enhancement in affinity
for the bivalent ligand compared to monovalent
ligand. This behavior demonstrates that
protein-protein interactions and aggregation are the
primary cause for affinity increases observed with
polyvalent saccharide ligands, and unambiguously
establishes a molecular basis for the cluster
glycoside effect.