Skip to content

Eyal Vardy

National Institute of Mental Health

4 papers in the library · 1,263 citations · publishing 2013-2014

Papers

Structural Features for Functional Selectivity at Serotonin Receptors

Science March 21, 2013 Daniel Wacker, Chong Wang, Vsevolod Katritch et al. 689 citations

Serotonin receptors are targets for drugs treating depression, obesity, and migraine headaches. Crystal structures of two serotonin receptor subtypes bound to antimigraine medications or a precursor of LSD reveal how subtle differences in ligand binding cause substantial differences in receptor signaling and biological responses. The structures show that the same ligand can activate one or both of the two main serotonin receptor signaling mechanisms, depending on which receptor it binds.

Structural Basis for Molecular Recognition at Serotonin Receptors

Science March 22, 2013 Chong Wang, Yi Jiang, Jinming Ma et al. 522 citations

Two research teams independently determined the crystal structures of two serotonin receptors bound to antimigraine drugs or a precursor of LSD. The structures show that subtle differences in how ligands bind to these receptors lead to substantial differences in the signals generated and the resulting biological responses. The same ligand can activate one or both of the two main serotonin receptor signaling mechanisms, depending on which specific receptor it binds to.

Michael acceptor approach to the design of new salvinorin A-based high affinity ligands for the kappa-opioid receptor.

European journal of medicinal chemistry October 6, 2014 Prabhakar R Polepally, Krzysztof Huben, Eyal Vardy et al. 28 citations

Salvinorin A, a compound from the plant Salvia divinorum, binds strongly and selectively to the κ-opioid receptor (KOR). A new series of salvinorin A derivatives with reactive Michael acceptor groups at C-2 was created to explore how the compound interacts with the receptor. Most of these derivatives retained high affinity for KOR, and some also bound to the μ-opioid receptor (MOR). None showed wash-resistant irreversible binding. Using the KOR crystal structure, mutagenesis data, and other methods, the researchers identified possible ways the new compounds interact with both KOR and MOR.

Kappa-opioid receptor-selective dicarboxylic ester-derived salvinorin A ligands.

Bioorganic & medicinal chemistry letters May 15, 2013 Prabhakar R Polepally, Kate White, Eyal Vardy et al. 24 citations

Salvinorin A, the active ingredient in the hallucinogenic plant Salvia divinorum, is nature's most potent hallucinogen and selectively activates the κ-opioid receptor. To explore how these compounds bind to specific receptors, researchers synthesized a series of dicarboxylic ester derivatives of salvinorin A and tested their binding affinity at κ-, δ-, and μ-opioid receptors. Most of the new compounds showed high affinity for the κ-opioid receptor. The methyl malonyl derivative 4 had the strongest binding, with a Ki of 2 nM, while analogues 5, 7, and 14 also exhibited significant affinity, with Ki values of 21, 36, and 39 nM respectively. These findings provide insights into brain chemistry and ligand-receptor interactions.