Computational Insights into the Interaction of Muscimol with Human Serum Albumin
Biointerface Research in Applied Chemistry December 15, 2024 DOI: 10.33263/briac146.132 (opens in new tab)
Study at a glance
AI-extracted from the abstract| Characteristics | Computational docking study Peer reviewed |
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| Key points | The authors report that muscimol binds preferentially to site III of human serum albumin with a binding energy of -6.56 kcal/mol, while sites I and II are less stable binding sites. Hydrogen bonds and van der Waals forces are identified as the main stabilizing interactions, and an unfavorable interaction with Ser-287 is proposed to explain the reduced stability at site I. |
Abstract
Muscimol (MCM) is a psychoactive compound derived from the Amanita muscaria mushroom. It is known for its hallucinogenic properties and is primarily responsible for the psychoactive effects of the mushroom. The interaction of bioactive compounds with plasma transport proteins greatly affects their pharmacological profile and, thus, their potential therapeutic effects. Accordingly, using computational approaches, we investigated the interaction of MCM with the primary carrier protein in humans, human serum albumin (HSA). The preferred binding site of MCM is suggested at site III of HSA (binding energy: 6.56 kcal/mol), with sites I and II acting as less stable possible binding sites. Hydrogen bonds and van der Waals forces primarily contributed to stabilizing the MCMHSA complexation, with possible involvement of ionic forces. An unfavorable interaction involving Ser-287 was identified as the cause of the reduced stability of MCM docking at site I.