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In this SpiroWebinars Autumn Series (Pushing Boundaries), we will be covering a topic that keeps us all awake at night: how to construct better molecules with better properties?Get to know us
Get to know us.
Prof. Dr. Kevin Brown, PhD
Recently named the James F. Jackson Professor of Chemistry at Indiana University.
Prof. Dr. Thierry Langer
University of Vienna, AT
Dr. Gerhard Müller
CSO Anavo Therapeutics, DE
Prof. Dr. Matthias Gehringer
University of Tuebingen, DE
At what time?
In this webinar Prof. Dr. Kevin Brown, PhD will give you an in-depth knowledge on the topic of Advances in the Synthesis and Design of New Classes of Strained Building Blocks
In his webinar, Prof. Thierry Langer will showcase the use of the SpiroChem 3D Fragment Library as well as the new SpiroSpaceTM compound collection for hit finding as well as for addressing difficult targets. Combining high performance virtual screening with LigandScout and well-designed sp3-enriched libraries gives excellent starting points for hit-to-lead programs and provides strong support for lead optimization phases.
Occasionally, the Medicinal Chemistry community tends to operate “under the lamp post”, i.e., there is hesitation to explore entire new areas of e.g., chemical space, chemical reactions, or target space.
The family of protein phosphatases is a rich but under-exploited source of therapeutically validated drug targets modulating signal transduction pathways. Unlike the kinase family, research and development activities have not yet yielded any approved small-molecule drugs against a member of that target class to date. Approximately 20 years ago, the phosphatase family was classified as undruggable. This was mainly driven by the failure of the industry-wide drug discovery efforts to develop PTP1B inhibitors.
Only few years ago, allosteric inhibitors against SHP2 have entered clinical trails. This has reawakened industry’s interest towards this neglected enzyme family. This Webinar will shed light on the kinase-phosphatase mystery, will deliver deeper insight on why the phosphatase family has been classified as undruggable, and will provide a perspective on how to successfully unlock the therapeutic value of the phosphatase family.
Protein kinases are now among the major drug targets and over 70 small molecule inhibitors have entered the market since the groundbreaking approval of imatinib (Gleevec) in 2001. Covalent inhibitors, which have gained traction in recent years, have proven particularly useful in the protein kinase field due to their superior potency, selectivity, and prolonged duration of action. Of the >500 human protein kinases, almost half are characterized by the presence of an accessible, non-conserved cysteine residue in or around the ATP binding site, which can be targeted by mild electrophiles termed covalent "warheads".
No Strain, No Gain: Advances in the Synthesis and Design of New Classes of Strained Building Blocks
Pharmacophore-based Virtual Screening: Examples Using The New SpiroChem Libraries
The kinase-phosphatase mystery: a prolific and an underexplored target family
Targeting Protein Kinases with Covalent Inhibitors
Matthias Gehringer is an Assistant Professor for Medicinal Chemistry and Associate Investigator in the Cluster of Excellence 'Image-guided and Functionally Instructed Tumor Therapies' (iFIT) at the University of Tübingen. After studying chemistry in Karlsruhe, Montpellier, and Heidelberg, he received his Ph.D. in Medicinal Chemistry from the University of Tübingen (group of Prof. Stefan Laufer). As a postdoc, he worked with Prof. Karl-Heinz Altmann at the Swiss Federal Institute of Technology (ETH) in Zürich on the total synthesis of bioactive natural products. His research focuses on protein kinase inhibitors and covalent targeting strategies.
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