Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 1 de 1
Filter
Add more filters










Database
Language
Publication year range
1.
ACS Chem Neurosci ; 8(8): 1681-1687, 2017 08 16.
Article in English | MEDLINE | ID: mdl-28514141

ABSTRACT

A series of analogues based on serine as lead structure were designed, and their agonist activities were evaluated at recombinant NMDA receptor subtypes (GluN1/2A-D) using two-electrode voltage-clamp (TEVC) electrophysiology. Pronounced variation in subunit-selectivity, potency, and agonist efficacy was observed in a manner that was dependent on the GluN2 subunit in the NMDA receptor. In particular, compounds 15a and 16a are potent GluN2C-specific superagonists at the GluN1 subunit with agonist efficacies of 398% and 308% compared to glycine. This study demonstrates that subunit-selectivity among glycine site NMDA receptor agonists can be achieved and suggests that glycine-site agonists can be developed as pharmacological tool compounds to study GluN2C-specific effects in NMDA receptor-mediated neurotransmission.


Subject(s)
Excitatory Amino Acid Agonists/pharmacology , Receptors, N-Methyl-D-Aspartate/agonists , Animals , Binding Sites , Dose-Response Relationship, Drug , Excitatory Amino Acid Agonists/chemistry , Glycine/metabolism , Glycine/pharmacology , Membrane Potentials/drug effects , Membrane Potentials/physiology , Molecular Docking Simulation , Molecular Dynamics Simulation , Oocytes , Patch-Clamp Techniques , Protein Binding , Protein Multimerization , Receptors, N-Methyl-D-Aspartate/metabolism , Recombinant Proteins/metabolism , Stereoisomerism , Xenopus laevis
SELECTION OF CITATIONS
SEARCH DETAIL
...