Tools to understand the mechanisms of protein binding to cell surface proteins are of interest to enable the manipulation of such proteins, such as for therapy and drug delivery. In particular, bioorthogonal techniques are of interest as they can be used to probe protein structure and function in their native environment with minimal structural perturbation, as described in Chapter 1. This work seeks to develop such bioorthogonally-designed materials (polymers and nanoparticles) in order to study adhesive proteins.

In Chapter 2, using controlled radical polymerisation and “click”-like chemistries, doubly-functionalised glycopolymers with sequential variation in carbohydrate density, side chain length and secondary functionality were synthesized to probe the binding activity of an adhesive pathogenic toxin (Vibrio cholerae toxin subunit B). This revealed a new approach whereby sterically large secondary units enabled selectivity towards a toxin to be introduced.

In chapter 3, a small (