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Discovery of a functionally selective serotonin 5-HT1A receptor agonist for the treatment of pain

Ullrich, A.; Schneider, J.; Braz, J. M.; Neu, E.; Staffen, N.; Stanek, M.; Blahova, J.; Hove, T.; Albert, T.; Allikalt, A.; Lober, S.; Bhardwaj, K.; Rodriguez-Rosado, S.; Fink, E. A.; Rasmussen, T.; Hubner, H.; Inoue, A. A.; Shoichet, B. K.; Basbaum, A.; Bottcher, B.; Weikert, D.; Gmeiner, P.

2023-09-14 pharmacology and toxicology
10.1101/2023.09.11.557127 bioRxiv
Show abstract

The G protein-coupled serotonin receptor 5-HT1AR mediates antinociception and may serve as a valuable target for the treatment of pain. Starting from a chemical library, ST171, a bitopic chemotype activating 5-HT1AR was evolved. In vitro pharmacological investigations of ST171 revealed potent and selective Gi activation (EC50 = 0.3 nM), with marginal Gs and {beta}-arrestin recruitment. Preclinical studies in mice showed that ST171 was effective in acute and chronic (inflammatory and neuropathic) pain models, without causing sedation. Comparison of cryo-EM structures of a 5-HT1AR-Gi complex bound to the functionally biased agonist ST171, with a structure bound to the functionally balanced agonist befiradol, showed that both ligands bind to the same orthosteric site, but address different exo-sites. The individual poses are associated with ligand-specific helical dispositions and rearrangements of microdomains. Complementation of these studies with molecular dynamics simulations allowed us to derive structural features associated with ST171s functional selectivity, a phenomenon that may be crucial to the discovery of more effective and safe GPCR drugs.

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