Our highly trained team has extensive experience in the application of theoretical models and data analysis to derive scalable descriptors of drug action, and better predict clinical efficacy.
Competitive, allosteric (using allosteric ternary complex (ATCM) models to quantify the cooperativity factor, α), two-step binding, avidity with bivalent ligands (e.g. antibodies), enzyme mechanisms (ordered, random, ping-pong) and enzyme inhibition profiling (tight-binding, mixed mode inhibition).
The operational model and quantification of ligand bias (eg ΔΔlogτ/KA), positive and negative allosteric action (using the operational ATCM to quantify the functional cooperativity factor, β).
Integrating the kinetics of binding and pathway activation/inactivation to build a better understanding of drug action over time. This knowledge can be invaluable in building and refining in vivo PK/PD models.
Kinetic and equilibrium models of binding, and avidity resulting from bivalency. Analysis of stimulus antagonism (e.g. cytokine antibody binding).