HIGH AFFINITY INHIBITORS OF SH3 DOMAIN-MEDIATED PROTEIN-PROTEIN INTERACTIONS

Intracellular protein recognition domains are important targets for drug design, as several forms of cancer and other proliferative diseases are tightly linked to signaling malfunctions. However, these domains have proven challenging targets to find compounds which bind with high affinity.

Researchers have addressed this challenge by studying proline-rich binding domains, the SH3 (Src-Homology 3) domain and the WW domain. They have discovered the basis for how these domains interact with their partner proteins. They have used this knowledge to design an SH3 inhibitor which binds with the highest affinity to date (~40 nM). Similar efforts should enable the design of inhibitors of other proline-rich binding domains in disease pathways.

If you would like to receive further information about this technology and potential licensing opportunities, please contact:

Joel B. Kirschbaum, Ph.D.
Director & Senior Technology Portfolio Manager
(415) 353-4462 phone
(415) 348-1579 fax
Joel Kirschbaum, Ph.D.

Reference: OTM Case #SF99-003