Year of Award

2024

Document Type

Dissertation

Degree Type

Doctor of Philosophy (PhD)

Degree Name

Pharmaceutical Sciences and Drug Design

Department or School/College

Division of Biological Sciences

Committee Chair

Kasper B. Hansen

Commitee Members

Richard Bridges, Travis Hughes, Jesse Hay, Katie Holick

Abstract

NMDA-type ionotropic glutamate receptors are widely expressed throughout the central nervous system and are critically involved in many healthy neuronal processes. Dysregulation of NMDA receptor activity underlies many disease pathologies, several of which benefit from treatment with antagonists, such as the FDA-approved channel blockers ketamine, memantine, and adamantine. NMDA receptors are composed of two glycine-binding GluN1 subunits and two glutamate-binding GluN2A-D subunits. The GluN2A-D subunits display distinct regional and developmental expression patterns, enabling region- or cell type-specific targeting of NMDA receptors through subunit-selective pharmacological intervention. There are several classes of subunit-selective negative allosteric NMDA receptor modulators, but the mechanisms of allosteric inhibition are complex and difficult to characterize. To provide deeper insights to the functional activity of GluN2A-selective negative allosteric modulators, we employ a multifaceted approach combining protein crystallography, pharmacological modeling, targeted mutagenesis, and electrophysiology to quantitatively compare receptor-modulator interactions. Implementing this strategy will improve analysis of structure-activity relationships and facilitate the rational structure-based design of novel NMDA receptor modulators with therapeutic potential in brain disorders.

Available for download on Thursday, June 18, 2026

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© Copyright 2024 James Scott Lotti