Kinases are among the most intensively pursued target families in drug discovery, yet the chemical matter screened against them remains surprisingly narrow. Conventional kinase-focused libraries are dominated by flat, heteroaromatic compounds, while saturated, three-dimensional molecules stay largely underexplored. That narrow structural diversity makes it harder to find genuinely novel chemotypes, reach alternative binding sites, and build inhibitors with better selectivity and drug-like properties.
About the webinar
Dr. Serghei Glinca, CEO of CrystalsFirst, will present a recent study in J. Chem. Inf. Model. that investigates natural product-like fragments as a source of unconventional kinase-binding chemistry. Using a high-performance crystallographic soaking system for protein kinase A, the researchers resolved 36 fragment-bound structures at a hit rate of 41%. The fragments showed diverse binding modes across the ATP and peripheral sites, including a previously unexplored allosteric binding opportunity and an unexpected protein conformational change.
What you will learn
- Campaign design: how the crystallographic screen against protein kinase A was set up and run.
- Binding beyond the ATP site: which protein-fragment complexes proved most intriguing, and what they reveal.
- Chemical space coverage: why saturated, spatially complex fragments sit apart from established kinase binders.
- Next steps: how three-dimensional, natural product-like fragments open new avenues for kinase drug discovery.
Who should attend
Medicinal and computational chemists, structural biologists, and fragment-based drug discovery teams working on kinases or on expanding the three-dimensionality of their screening libraries.
|
Unable to join live? Register anyway and we will send you the recording. Browse all sessions on the BioSolveIT webinars page.