Kinase Inhibitors with Tailored Binding Kinetics by Fragment-Based Design

Peter Sennhenn, Head of Medicinal Chemistry, Proteros fragments GmbH

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Launch presentation

Abstract

Transient or weak biological interactions (dissociation constant: KD > µM), either working alone or together, play fundamental roles in sustaining life and it is only recently we are starting to realize how they act and their intricate function in complex biological processes. This fact has important consequences for drug discovery as we can question the central dogma of finding high-affinity (typically nanomolar) binders to a single target. Development of a “transient” drug/fragment to a single target or multiple targets is an interesting approach to profit on the understanding of a transient biological system. Another potential benefit is the notion that side-reactions of drugs may be explained to some extent by the occurrence of weak binding reactions. However, a major challenge is to “see” the weak binders in the laboratory but new technologies are emerging which can screen and define the characteristics of a transient binder both in terms of affinity and kinetics.

In my presentation, I will discuss the basic ideas behind the concepts of transient drugs/fragments, show potential screening methods to find them and present some possible areas for development of the transient drug.

Launch presentation