Selecting optimal drug-intervention in a pathway involving receptor tyrosine kinases (RTKs)

Abstract

A recently developed system-pharmacological model for the dynamics of receptor tyrosine kinases is used to compare different targets for drug action: one aiming at binding endogenous ligand needed for phosphorylation and another binding receptors at their kinase domains and thus preventing them to generate phosphorylation. We obtain quantitative estimates for the effectivity of the inhibitor which demonstrate the influence of drug-properties such as dose, affinity to target and drug-elimination rates.