Antagonistic action on NMDA/GluN2B mediated currents of two peptides that were conantokin-G structure-based designed.

ABSTRACT:

Background

The GluN2B subunit of the N-methyl-D-aspartate receptor (NMDAr) modulates many physiological processes including learning, memory, and pain. Excessive increase in NMDAr/GluN2B activity has been associated with various disorders such neuropathic pain and neuronal death following hypoxia. Thus there is an interest in identifying NMDAr antagonists that interact specifically with the GluN2B subunit. Recently based on structural analysis between the GluN2B subunit and conantokin-G, a toxin that interacts selectively with the GluN2B subunit, we designed various peptides that are predicted to act as NMDAr antagonists by interacting with the GluN2B subunit. In this study we tested this prediction for two of these peptides EAR16 and EAR18.

Results

The effects of EAR16 and

SUBMITTER: Reyes-Guzman EA 

PROVIDER: S-EPMC5433008 | biostudies-literature | 2017 May

REPOSITORIES: biostudies-literature