Kinase Inhibitor Discovery

In 2017 we saw several kinase inhibitors approved by the FDA. Case studies or histories of several of these drugs will be presented at this year’s Kinase Inhibitor Discovery conference at the Discovery on Target event in Boston to mark this success. In addition results with several promising candidates in the pipeline will be presented. Special coverage will be given to work dedicated to binding kinetic studies with kinases and other issues that remain a challenge including selectivity. Attend to learn more.

Final Agenda

Thursday, September 27

11:50 am Conference Registration Open (Foyer)


12:20 pm Plenary Keynote Program (Constitution Ballroom)

2:00 Refreshment Break in the Exhibit Hall with Poster Viewing (Grand Ballroom)

Clinical And Advanced Inhibitors
Constitution A

2:45 Welcome Remarks

Victoria Mosolgo, Conference Producer, Cambridge Healthtech Institute

2:50 Chairperson’s Opening Remarks

Campbell McInnes, PhD, Professor, Drug Discovery and Biomedical Sciences, University of South Carolina

2:55 Cancer Drug Resistance, Challenge and Opportunity – The Osimertinib Story

Stephen Fawell, PhD, Vice President, Head Oncology iScience, AstraZeneca

First line EGFR inhibitors like gefitinib are highly active in EGFRmt NSCLC, however most patients eventually relapse with drug resistant disease of which the majority are driven by a second T790M mutation. Osimertinib, a potent and selective covalent inhibitor was specifically designed to target this form of the receptor. The combination of a well designed active drug and a clear patient selection strategy led to one of the fastest approvals of an Oncology drug.

3:25 Illuminating the Darkness…PKC Inhibitors for Metastatic Uveal Melanoma

Michael Visser, PhD, Group Leader, Senior Investigator, Novartis Institutes for BioMedical Research, Inc.

Uveal Melanoma (UM) is the most common primary intraocular malignancy of the adult eye, with an incidence of five to six cases per million. Despite aggressive local management of primary UM, the development of metastases is common and occurs in ~50% of patients. There are currently no effective treatment options for metastatic disease and median survival is around nine months. Genetic analysis of UM samples reveals the presence of activating mutations in the Gq alpha subunits, GNAQ and GNA11. One of the key downstream targets of the constitutively active Gq alpha subunits is the protein kinase C (PKC) signaling pathway. We describe the discovery of NVP-LXS196, a potent, selective PKC inhibitor. The lead series was optimized for kinase and off target selectivity to afford a compound that is rapidly absorbed and well tolerated in pre-clinical species. NVP-LXS196 is currently in Phase I clinical trials to assess the safety, tolerability and pharmacokinetic profile in metastatic uveal melanoma patients where encouraging early activity has been observed.

3:55 Sensors for Continuous Monitoring of Protein Kinase & Phosphatase Activity

Erik Schaefer, President, AssayQuant Technologies

AssayQuant® is combining chelation-enhanced fluorescence, using the sulfonamido-oxine (Sox) chromophore, with high-throughput peptide synthesis methods to identify optimized physiologically-based substrates for measuring the activity of protein kinases and phosphatases. The result is a simple yet powerful method that allows continuous, quantitative and homogenous detection of activity using recombinant enzymes or crude cell or tissue lysates. This approach provides a quantum improvement in assay performance and productivity needed to accelerate discovery and drug development efforts.

4:25 Refreshment Break in the Exhibit Hall with Poster Viewing (Grand Ballroom)

Clinical And Advanced Inhibitors (CONT.)
Constitution A

5:00 ARQ 531, a Reversible BTK Inhibitor Exhibits Distinct Kinase Selectivity and Demonstrates Potent Anti-Tumor Activity in Ibrutinib Resistant Tumor Models

Sudharshan Eathiraj, PhD, Senior Lead Investigator, Translational Medicine, ArQule, Inc.

ARQ 531 is an ATP competitive reversible inhibitor of BTK. Kinase selectivity profile combined with pathway analysis data suggests that ARQ 531 targets multiple oncogenic signaling pathways and potently inhibits tumor growth in the mouse xenografts of cell lines primarily resistant to previously approved BTK inhibitor, ibrutinib. ARQ 531 monotherapy is currently being investigated in a Phase 1 dose-escalation study in B-cell hematologic malignancies.

5:30 Full Kinome and Cancer Cell Panel Profiling of All Kinase Inhibitor Drugs Approved for Clinical Use

Guido Zaman, PhD, Managing Director & Head of Biology, Netherlands Translational Research Center B.V.

All small molecule kinase inhibitors approved for clinical use were profiled on a panel of 275 biochemical kinase assays and 102 cancer cell line proliferation assays (Oncolines). Novel genomic biomarkers predictive of drug response in human tumor cells were discovered. Comparative analyses of biochemical and cellular profiling data yielded new insight into the mechanism of action of different kinase inhibitor drugs acting via the same primary target or signaling pathway.

Covalent Inhibitors
Constitution A

6:00 The Meisenheimer Complex as a Novel Paradigm in Drug Discovery: Targeting PLK1 through a Novel Covalent Mechanism

Campbell McInnes, PhD, Professor, Drug Discovery and Biomedical Sciences, University of South Carolina

This talk will describe novel inhibitors of PLK1 kinase activity that inhibit through the unique covalent strategy that reversibly inhibits kinase activity by formation of a Meisenheimer Complex. The discovery and optimization of these inhibitors is described in addition to confirmation of their on-target anti-tumor mode of action through selective PLK1 inhibition.

6:30 Dinner Short Course Registration (Foyer)

9:30 Close of Day

Friday, September 28

7:00 am Registration Open (Foyer)

7:30 Interactive Breakfast Breakout Discussion Groups

Room: Constitution A

Grab a cup of coffee and join a breakout discussion group. These are informal, moderated discussions with brainstorming and interactive problem solving, allowing participants from diverse backgrounds to exchange ideas and experiences and develop future collaborations around a focused topic.

Table 7:Challenges in Kinase Inhibitor Discovery

Moderator: Istvan Enyedy, PhD, Computational Chemistry, Biogen

  • Selectivity for safety
  • Blood-brain barrier permeability

Table 8: Kinase Targets for Cancer Immunotherapy

Moderator: Guido Zaman, PhD, Managing Director & Head of Biology, Netherlands Translational Research Center B.V.

  • What are the new and promising kinase targets for cancer immunotherapy?
  • Lessons learned from combination studies with immune checkpoint modulators
  • Technologies and approaches for target identification and validation 

 

Selective Inhibitors & Promising Candidates
Constitution A

8:30 Chairperson’s Remarks

Istvan Enyedy, PhD, Computational Chemistry, Biogen

8:35 Discovery of ATR Inhibitor BAY 1895344 with Favorable PK Properties and Promising Anti-Tumor Efficacy in Monotherapy and Combination in Preclinical Tumor Models

Ulrich Luecking, PhD, Principal Scientist, Medicinal Chemistry, Bayer

The identification of ATR inhibitor BAY 1895344 is reported. In vitro, BAY 1895344 was shown to be a very potent and highly selective ATR inhibitor, which potently inhibits proliferation of a broad spectrum of human tumor cell lines. BAY 1895344 revealed good bioavailability across species. Moreover, BAY 1895344 demonstrated potent anti-tumor efficacy in monotherapy in DNA damage response deficient tumor models as well as in combination treatment with DNA damage-inducing and DNA repair-compromising therapies.

9:05 Discovery of Novel, Soft JAK Kinase Inhibitors for Topical Treatment of Psoriasis

Daniel R. Greve, PhD, Senior Manager, Head of Medicinal Chemistry, LEO Pharma A/S

The presentation covers our efforts in a recent research project aiming for novel, selective pan-JAK inhibitors to treat psoriasis topically. The small molecule inhibitors have a pharmacokinetic profile that allows for high local exposure combined with low systemic exposure, by optimizing human hepatic clearance. The best compounds are efficacious in our mouse xenograft model of plaque psoriasis, while being rapidly cleared from systemic circulation.

9:35 Discovery of AS-871, a Selective and Non-Covalent BTK Inhibitor for the Treatment of Rheumatoid Arthritis

Masaaki Sawa, PhD, CSO, Carna Biosciences, Inc.

We have developed a novel non-covalent inhibitor of BTK through the optimization of a lead compound which was derived from our SYK/BTK dual inhibitor program. During the lead optimization, we employed a dual screening approach using two conformationally different BTK proteins, an activated form of BTK and an unactivated form of BTK to enhance the selectivity. AS-871 displayed potent inhibitory activities in cellular assays and demonstrated significant efficacies in several i n vivo models.

10:05 Coffee Break in the Exhibit Hall with Poster Viewing and Poster Competition Winner Announced (Grand Ballroom)

Phosphatases

10:45 A Genomic Perspective on Protein and Lipid Phosphatases

Gerard Manning, PhD, Director, Bioinformatics and Computational Biology Genentech

Kinases and phosphatases jointly control most biological pathways. Many phosphatases are altered in disease but have been challenging to target. We have cataloged all human protein and lipid phosphatases (the phosphatome) to serve as a global resource for understanding all phosphorylation events, and to derive new targets and biomarkers. I will review our findings and potential for new therapeutic development..

11:15 Novel Inhibitor Design Concepts for Protein Kinases and Phosphatases

Gerhard Mueller, PhD, CSO, Gotham Therapeutics

The last 20 years of research on small molecule protein kinase inhibitors resulted in approximately 40 small molecule kinase inhibitors that received market approval. Apart from the traditional design paradigm, i.e. optimizing compounds to competitively bind into the ATP site, a number of allosteric inhibitor binding modalities have been discovered that allow to engineer molecular properties such as target residence time. In contrast to the kinase field, the target family of protein phosphatases is and remains an underexplored area even though individual members are well-validated drug targets for therapeutic intervention into a number of disease states. The medicinal chemistry approaches that have been chosen to inhibit protein phosphatases will be highlighted, again emphasizing the relevance of allosteric binding mechanisms over traditional active site-directed design approaches.

11:45 Exploring Kinase Inhibitor Selectivity and Affinity in Live Cells Using NanoBRET

Matthew Robers, Senior Research Scientist, Group Leader, Biology, Promega Corporation

Yuren Wang, Director, Pharmacology and QC, Cell-Based Assay Group, Reaction Biology Corp.

We will describe the application of an energy transfer technique (NanoBRET) that enables the first quantitative approach to broadly profile fractional occupancy and compound affinity for kinases in live cells. Through a collaboration with Reaction Biology Corp (RBC), the NanoBRET technology has been scaled into a high-throughput cell-based profiling format. The validated Promega’s NanoBRET cell-based assay technology platform is compatible with RBC’s broad spectrum in vitro biochemical radioactive kinase assay platform.

12:15 pm Session Break

12:25 Enjoy Lunch on Your Own

1:15 Refreshment Break in the Exhibit Hall with Poster Viewing (Grand Ballroom)

Binding Kinetics And Profiling
Constitution A

1:55 Chairperson’s Remarks

Guido Zaman, PhD, Managing Director & Head of Biology, Netherlands Translational Research Center B.V.

2:00 Kinetic Selectivity and Target Vulnerability in Drug Discovery

Peter Tonge, PhD, Professor, Chemistry, Stony Brook University

Since a drug can bind to two targets with the same affinity but different on and off rates, drug selectivity has both a thermodynamic and a kinetic component. Using systems such as Bruton’s tyrosine kinase as an example, we discuss the utility of kinetic selectivity, and the role of target turnover and target vulnerability in the translation of kinetic selectivity to in vivo drug activity.

2:30 Conformational Adaption May Explain the Slow Dissociation Kinetics of Roniciclib (BAY 1000394), a Type I CDK Inhibitor with Kinetic Selectivity for CDK2 and CDK9

Christian Stegmann, PhD, Management Support, Research & Development, Pharmaceuticals, Bayer AG

Roniciclib (BAY 1000394) is a type I pan-CDK (cyclin-dependent kinase) inhibitor which has revealed potent efficacy in xenograft cancer models. We could show that roniciclib displays prolonged residence times on CDK2 and CDK9, whereas residence times on other CDKs are transient, thus giving rise to a kinetic selectivity of roniciclib. In tumor cells, the prolonged residence times of roniciclib on CDK2 and CDK9 are reflected in a sustained inhibitory effect on retinoblastoma protein (RB) phosphorylation, indicating that the target residence time on CDK2 may contribute to sustained target engagement and antitumor efficacy.

3:00 A Kinase Platform for the Discovery of Reversible and Covalent Kinase Inhibitors

Igor Mochalkin, PhD, Associate Director, EMD Serono

Protein kinases play an important role in signaling pathways that control cell growth, metabolism, proliferation and apoptosis, and the dysregulation of kinase functions can fuel cancers and other diseases. To identify novel, potent and selective kinase inhibitors for the treatment of oncological and immunological disorders, we established a Kinase Platform Project team to leverage kinase-target profiling, de novo design, fragment screening and covalent approaches targeted to individual kinases and kinase mini-panels. In this presentation, we highlight our implementation of drug discovery technologies that led to the identification and development of two clinical candidates, evobrutinib and M2698.

3:30 Strategies for Designing Selective Kinase Inhibitors

Istvan Enyedy, PhD, Computational Chemistry, Biogen

Designing selective kinase inhibitors has been challenging. The desired selectivity of a kinase inhibitor depends on the therapeutic area. Polypharmacology is often desired in oncology, while highly selective inhibitors are usually needed for other therapeutic areas. Strategies for designing selective inhibitors vary from targeting residues that are less conserved to exploiting differences in the flexibility of the kinase domain when selectivity among isoforms is desired.

4:00 Close of Conference