General anesthesia has been widely utilized for over a century, yet its mechanism for action remains largely unknown. Experimental evidence indicates that Gamma Aminobutyric Acid Type-A Receptors (GABAA-R) from the family of Ligand-Gated Ion Channels (LGIC) are targets of anesthetic action. Several LGICs from this family were analyzed using the Computed Atlas of Surface Topography of proteins (CASTp) and eF-surf programs to determine the structure and properties of likely anesthetic binding cavities. This data then will be used to calculate the binding energy and the preferred geometry of the anesthetic propofol in the GABAA-R binding cavity. Accurate modeling of these anesthetic-protein interactions can aid in the search for safer, more effective anesthetics.

Theoretical investigation of anesthetic binding sites in ligand-gated ion channels

245th National Meeting (2013)

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