Derivatives of (R)-3-(5-Furanyl)carboxamido-2-aminopropanoic Acid as Potent NMDA Receptor Glycine Site Agonists with GluN2 Subunit-Specific Activity

J Med Chem. 2022 Jan 13;65(1):734-746. doi: 10.1021/acs.jmedchem.1c01810. Epub 2021 Dec 17.

Abstract

NMDA receptors mediate glutamatergic neurotransmission and are therapeutic targets due to their involvement in a variety of psychiatric and neurological disorders. Here, we describe the design and synthesis of a series of (R)-3-(5-furanyl)carboxamido-2-aminopropanoic acid analogues 8a-s as agonists at the glycine (Gly) binding site in the GluN1 subunit, but not GluN3 subunits, of NMDA receptors. These novel analogues display highly variable potencies and agonist efficacies among the NMDA receptor subtypes (GluN1/2A-D) in a manner dependent on the GluN2 subunit. Notably, compound 8p is identified as a potent partial agonist at GluN1/2C (EC50 = 0.074 μM) with an agonist efficacy of 28% relative to activation by Gly and virtually no agonist activity at GluN1/2A, GluN1/2B, and GluN1/2D. Thus, these novel agonists can modulate the activity of specific NMDA receptor subtypes by replacing the full endogenous agonists Gly or d-serine (d-Ser), thereby providing new opportunities in the development of novel therapeutic agents.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Carrier Proteins / agonists*
  • Excitatory Amino Acid Agonists / chemical synthesis*
  • Excitatory Amino Acid Agonists / pharmacology*
  • Glycine / drug effects*
  • Humans
  • Membrane Proteins / agonists*
  • Models, Molecular
  • Nerve Tissue Proteins / agonists*
  • Receptors, N-Methyl-D-Aspartate / agonists*
  • Structure-Activity Relationship
  • Xenopus
  • Xenopus laevis

Substances

  • Carrier Proteins
  • Excitatory Amino Acid Agonists
  • GPRIN2 protein, human
  • Membrane Proteins
  • Nerve Tissue Proteins
  • Receptors, N-Methyl-D-Aspartate
  • Glycine