Adhirons as pharmacophore templates

The development of molecular tools to modulate protein function is an attractive approach for understanding basic biological questions as the tools not only allow validation of targets in biological systems, but they can also help inform the complexities of protein dynamics and conformational changes.

Recent research has illustrated that protein-protein interfaces and allosteric regions of protein surfaces contain 'hot-spots/regions' that confer most of the binding energy and show conformational adaptivity.

Identifying hot-regions and associated conformers is difficult but critical to fully understand protein function, ultimately leading to effective ligand identification.

Here we propose to use a unique disruptive approach to simultaneously identify hot-regions, conformers and, in addition, a template upon which to build ligands.

Specifically, we will isolate Adhiron reagents against propriety Syngenta targets to help understand the functional consequences of locking proteins in different conformations, with the potential of identifying hotspots of proteins for future development of inhibitors.