Uppsala, Sweden, 26 May 2015
Beactica, the Swedish fragment-based drug discovery company, today announced the publication of a key paper in Proceedings of the National Academy of Sciences*. The paper describes important work towards the discovery of novel drugs targeting ligand-gated ion channels, a significant family of drug targets involved in various neurological diseases. The study showcases the ability of Beactica’s drug discovery platform to successfully identify and utilize novel binding sites on proteins of therapeutic relevance.
The publication outlines work of importance for the a7 nicotinic acetylcholine receptor which plays a crucial role in fast synaptic signalling in the central and peripheral nervous system. Specifically, the Beactica scientists applied an efficient and innovative SPR biosensor-based screening approach to identify novel allosteric modulators to this challenging drug target. Allosteric modulators are structurally different to native ligands of a receptor, and bind to other sites, resulting in alternative modes of action with different functional effects. The interaction characteristics of the identified allosteric modulators, as well as the structural details of their binding to the target, and their functional effects on signalling, have been analysed in detail by Beactica researchers and their collaborators. The study paves the way for development of novel allosteric modulators with therapeutic potential in a diverse range of inherited neurological disorders, including epilepsy. Beactica’s approach for the identification of allosteric modulators can be applied also to other types of proteins, such as enzymes. The research was performed in collaboration between Beactica and scientists at Janssen Research & Development, a division of Janssen Pharmaceutica NV (Belgium), Katholieke Universiteit Leuven (Belgium) and HiQScreen Sàrl (Switzerland).
For additional information please contact Dr Per Källblad, Beactica CEO, +46 18 560880.
* Publication reference
Spurny et al. Molecular blueprint of novel allosteric binding sites in the agonist-binding domain of the a7 nicotinic acetylcholine receptor, PNAS, 2015, 112(19):E2543–E2552 (DOI:10.1073/pnas.1418289112).
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