TY - JOUR
T1 - Design of a new psychedelic quipazine analog with therapeutic efficacy and potentially fewer side effects
AU - Younkin, Jason
AU - Bansode, Ajay H.
AU - Saha, Somdatta
AU - Paymode, Archana
AU - Maltman, Jessica L.
AU - Jones, Charles B.
AU - Silverman, Justin M.
AU - Buzzi, Belle
AU - Jaster, Alaina M.
AU - Fiorillo, Michael
AU - Rolquin, Jeremy
AU - Miller, George D.
AU - Abedi, Roya
AU - Kang, Minho
AU - Gaines-Smith, Maya
AU - Valenzuela Lesme, Enrique I.
AU - Embretsen, Mattias
AU - Wolstenholme, Jennifer T.
AU - Glennon, Richard A.
AU - Akbarali, Hamid I.
AU - Damaj, M. Imad
AU - Ramsey, I. Scott
AU - Dukat, Małgorzata
AU - González-Maeso, Javier
N1 - Publisher Copyright:
© 2026 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science.
PY - 2026/7/21
Y1 - 2026/7/21
N2 - Psychedelics that target serotonin 2A receptors (5-HT2ARs) hold therapeutic promise for neuropsychiatric disorders but are often hindered by off-target actions. The 5-HT2AR agonist quipazine also activates 5-HT3R, which contributes to undesirable side effects. Here, we developed VCU-1012, a quipazine-based, structurally distinct 5-HT2AR agonist devoid of 5-HT3R activity. VCU-1012 was developed by applying a strategic chemical design that combined deconstruction to pinpoint the nitrogen atom critical for 5-HT2AR activation with structure-activity relationship studies to minimize 5-HT3R agonism. We showed that VCU-1012 modulated dendritic spine structural plasticity in the frontal cortex and produced antidepressant-like effects in mice through 5-HT2AR without activating 5-HT3R, thereby avoiding the gastrointestinal side effects of quipazine. In addition, our molecular modeling and mutant analysis suggested that VCU-1012 interacted in the canonical orthosteric binding pocket of 5-HT2AR. Together, these findings establish VCU-1012 as a potential therapeutic agent with reduced gastrointestinal impact, emphasize how differences in ligand-receptor interactions influence ligand positioning in the receptor binding pocket, and provide guidance for designing psychedelics with targeted therapeutic benefits.
AB - Psychedelics that target serotonin 2A receptors (5-HT2ARs) hold therapeutic promise for neuropsychiatric disorders but are often hindered by off-target actions. The 5-HT2AR agonist quipazine also activates 5-HT3R, which contributes to undesirable side effects. Here, we developed VCU-1012, a quipazine-based, structurally distinct 5-HT2AR agonist devoid of 5-HT3R activity. VCU-1012 was developed by applying a strategic chemical design that combined deconstruction to pinpoint the nitrogen atom critical for 5-HT2AR activation with structure-activity relationship studies to minimize 5-HT3R agonism. We showed that VCU-1012 modulated dendritic spine structural plasticity in the frontal cortex and produced antidepressant-like effects in mice through 5-HT2AR without activating 5-HT3R, thereby avoiding the gastrointestinal side effects of quipazine. In addition, our molecular modeling and mutant analysis suggested that VCU-1012 interacted in the canonical orthosteric binding pocket of 5-HT2AR. Together, these findings establish VCU-1012 as a potential therapeutic agent with reduced gastrointestinal impact, emphasize how differences in ligand-receptor interactions influence ligand positioning in the receptor binding pocket, and provide guidance for designing psychedelics with targeted therapeutic benefits.
UR - https://www.scopus.com/pages/publications/105045911913
U2 - 10.1126/scisignal.adw6055
DO - 10.1126/scisignal.adw6055
M3 - Article
C2 - 42479815
AN - SCOPUS:105045911913
SN - 1945-0877
VL - 19
JO - Science Signaling
JF - Science Signaling
IS - 947
M1 - eadw6055
ER -