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Wednesday, June 23

8:00 am Morning Coffee

Structure-Based Design 

8:25 Chairperson’s Remarks

Natasja Brooijmans, Ph.D., Principal Research Scientist, Pharmaceutical Chemistry, Wyeth

8:30 In Silico Structure Based Design of Non-ATP Competitive Kinase Inhibitors

Thomas Chan, CSO, ArQule, Inc.

It is a rare occurance to discover highly selective ATP-mimetic inhibitors since the ATP binding sites of kinases are usually conserved across several enzyme families. Typically, approaches that involve high-throughput screening takes time and resouces because of a very low hit rate. ArQule has developed a drug discovery platform that can rapidly identify potent and specific inhibitors against selected kinases. This technology has shortened early drug development timelines by 50% or greater, in addition to identifying novel chemical space to accommodate inhibitor design.

9:00 Supporting Structure-Based Drug Design: MAPKAP Kinase 2 as a Case Study

Maria A. Argiriadi, Ph.D., Principal Scientist, Molecular Pharmacology, Abbott Laboratories

9:30 Enabling Kinome-Wide Structure-Based Drug Discovery

Natasja Brooijmans, Ph.D., Principal Research Scientist, Pharmaceutical Chemistry, Wyeth

Due to their importance in many signaling pathways, kinases have become important drug targets for many diseases. Although a large number of kinase catalytic domain crystal structures are available through the public domain, it is not straightforward to query structures across the human kinome or to analyze and compare large numbers of kinase structures. We developed a Kinase Knowledge Base (KKB), which integrates structural data, kinase-specific annotations, and biological data. These annotations enable a large number of queries, and the retrieved structures can subsequently be visualized and analyzed. The utility and power of an enhanced structural database such as KKB will be illustrated through a number of use cases.

10:00 Networking Coffee Break

10:45 Structure-Based Drug Design Enables Conversion of a DFG-in Binding CSF-1R Kinase Inhibitor to a DFG-out Binding Mode

Atli Thorarensen, Ph.D., Associate Research Fellow, Pfizer, Inc.

The talk will describe the utility of structure-based drug design (SBDD) in shifting the binding mode of an HTS hit from a DFG-in to a DFG-out binding mode resulting in a of novel potent CSF-1R kinase inhibitors suitable for lead development.

11:15 New Trends and Opportunities in Kinase Inhibitors Design

Fabio Zuccotto, Ph.D., Computational Sciences, Chemical Core Technologies Department, Nerviano Medical Sciences

Generally, given the complex role of kinases in cancer, in the discovery of novel kinase inhibitors a multitarget strategy might be more effective than a strategy based on the inhibition of a single target. However a general promiscuity is highly undesirable due to potential toxicity linked to off-target activity. Hence the need of developing inhibitors that are not necessarily active against a single kinase but that are characterized by a specific activity profile that can guarantee efficacy and safety. Different design strategies that could be implemented to achieve the desired selectivity profile are discussed, in particular new strategies in targeting the DFG-in form of the kinase.

11:45 Lunch on Your Own 

Novel Platforms and Technologies 

1:10 pm Chairperson’s Remarks

1:15 Inhibition of Kinases by Deuterated Imidazole Compounds

Colin Kenyon, Group Leader, Biosciences, CSIR

Kinases are inhibited by a number of imidazole compounds. The deuteration of these compounds leads to an increase in the level of inhibition. The mechanism of interaction of these compounds with kinases can be elucidated from the kinetic isotope effect and site directed mutagenesis.

1:45 Adaptive Protein and Phosphoprotein Networks which Promote Therapeutic Sensitivity or Acquired Resistance

John Haley, Ph.D., Senior Research Director, Translational Research, OSI Pharmaceuticals

Multiple signal transduction pathways can be concurrently active within a single cell, and extensive crosstalk can occur between RTKs. Understanding pathway crosstalk and feedback control is vital to guide the rational combination of approved and experimental anti-cancer agents. The mechanisms of RTK cooption and reciprocal RTK activation impacting targeted drug sensitivity and resistance will be discussed.

2:15 Targeting Inactive Kinase Conformations 

Daniel Rauh, Ph.D., Group Leader, Molecular Physiology, Chemical Genomics Centre of the Max Planck Society 

The complexity of kinase biology is controlled by layers of regulatory mechanisms involving different combinations of post-translational modifications, intramolecular contacts, and intermolecular interactions. Ultimately, these mechanisms achieve their effect by favoring particular conformations that promote or prevent the kinase domain from catalyzing protein phosphorylation. A more detailed understanding of the structural principles that regulate protein kinase activity allowed us to develop a novel fluorescence-based binding assay (FLiK) for the identification and optimization of inhibitors that stabilize enzymatically incompetent kinase conformations. 

2:45 Networking Refreshment Break

3:15 A Novel Platform Based Approach to Silence Kinase Drug Targets Using Covalent Inhibitors

Mariana Nacht, Ph.D., Director of Biology, Avila Therapeutics, Inc.

3:45 Mapping Protein Kinase Networks and Drug Interactions with Protein Microarrays and Predictive Bioinformatics

Steven Pelech, President & CSO, Medicine, Kinexus; Professor, University of British Columbia

Using an 800 antibody microarray and predictive kinase substrate phosphorylation site consensus sequence profiling, Kinexus has developed a novel method to identify physiological substrates of over 388 target kinases, the sites that are phosphorylated and phospho-site-specific antibodies for their detection by immunoblotting. Kinexus has created free access, on-line knowledgebases with detailed information on 516 human protein kinases, 140 human protein phosphatases and over 70,000 confirmed human phosphorylation sites. Using bioinformatics approaches, Kinexus has predicted the identity of 500,000 human phosphorylation sites, investigated their evolutionary analysis in 22 other species to identify the most functionally relevant, and the deduced the specificity determinants for about 500 protein kinases to predict which of the kinases most likely target these phospho-sites.

4:15 End of Conference