• Preclinical stage development program – molecular modeling, synthesis and biochemical screening
• Tubulin isotype selectivity seen in binding assays
• Status: Lead evaluation and selection is on-going
• IP: Multiple US and international patent applications (since 2004)
• Development Plan: Nominate lead candidate for further evaluation in animal models
• Estimated Market Potential: >$8B

Tublin Database

Based on analysis of tubulins from over 500 sources, structural similarities and significant differences in physical properties have been found among the various forms of tubulin, including in the binding sites of paclitaxel and colchicines.

Tubulin structural differences related to drug resistance have been identified.

Enables design of novel chemical entities with highly selective binding tubulin isotypes.

Tublin Isotypes

Tubulin isotype compositions vary by cell type.

Cancer cells express isotypes whose distribution in normal tissues are rare.

Drug sensitivity and resistance are isotype-dependent.

Differences between tubulin isotypes have been identified, which enables testing drugs for efficacy against unique tubulin isotypes.

The ability of paclitaxel and other microtubule-binding drugs to suppress the dynamics of microtubule formation and shortening is tubulin isotype-specific.

Clinical implications of developing therapeutics against specific tubulin isotypes:

• Higher affinity will translate to greater efficacy
• Higher selectivity will translate to less toxicity
• Provides the opportunity to enrich trials for patients with specific isotypes to which agents are targeted