All biological processes involving biochemical reactions and relationships which are dependent on structure-function are driven or limited by intermolecular interactions. Researchers working within drug discovery for both small and large molecules have a primary requirement to understand the interactions of their candidate molecules with drug target protein molecules. The binding of two molecules, both in terms of strength and stoichiometry, provides a wealth of information which can help direct the rank-ordering of candidates.
The way in which two molecules interact with one another can be simple and straightforward, or may be much more complex - affected by other intermolecular interactions such as hydrogen bonding, hydrophobic and Van der Waals forces, and electrostatic interactions. Ideal for monitoring binding interactions are label-free, tag-free, direct measurement techniques which produce reliable, high-quality data, even for complex interactions.
Malvern Panalytical provides label-free, gold standard technology to act as a universal tool for studying both small molecule:protein and protein:protein interactions:
- Thermodynamic characterization of the relationship between two molecules
- Understanding and characterizing enzymatic reactions, to assist with research into disease pathways, drug discovery and the development of biofuels