AMPA (GluR2) receptor inhibitor peptide that inhibits the interaction between the C-terminus of the GluR2 subunit and N-ethylmaleimide-sensitive fusion protein (NSF). It reduces AMPA currents
CAT No: R0922
CAS No:243843-42-7
Synonyms/Alias:pep2m;243843-42-7;GluR2m;L-Glutamine,L-lysyl-L-arginyl-L-methionyl-L-lysyl-L-valyl-L-alanyl-L-lysyl-L-asparaginyl-L-alanyl-;KRMKVAKNAQ;(2S)-5-amino-2-[[(2S)-2-[[(2S)-4-amino-2-[[(2S)-6-amino-2-[[(2S)-2-[[(2S)-2-[[(2S)-6-amino-2-[[(2S)-2-[[(2S)-2-[[(2S)-2,6-diaminohexanoyl]amino]-5-(diaminomethylideneamino)pentanoyl]amino]-4-methylsulfanylbutanoyl]amino]hexanoyl]amino]-3-methylbutanoyl]amino]propanoyl]amino]hexanoyl]amino]-4-oxobutanoyl]amino]propanoyl]amino]-5-oxopentanoic acid;GluR2m, G10;AKOS024456690;PD079074;S-243843-42-7;
pep2m is a synthetic peptide compound designed for advanced biochemical research and experimental applications. As a member of the peptide family, it is characterized by a specific amino acid sequence that enables targeted interactions with proteins, enzymes, or cellular receptors. Its defined structure and customizable properties make it a valuable tool for probing molecular mechanisms, modulating biological pathways, and supporting the development of new assay systems. Researchers value pep2m for its reliability, reproducibility, and versatility in a range of laboratory and preclinical contexts, where precise peptide-based interventions are required to elucidate complex biological processes.
Peptide signaling studies: As a research peptide, pep2m is frequently employed in the investigation of peptide-mediated signaling pathways. Its sequence may be tailored to mimic, inhibit, or otherwise modulate endogenous peptide ligands, enabling scientists to dissect the functional roles of specific signaling molecules. By introducing pep2m into cell-based or in vitro systems, researchers can monitor downstream effects on receptor activation, second messenger cascades, or gene expression profiles, thus gaining detailed insights into the molecular underpinnings of physiological and pathological processes.
Protein interaction assays: The defined structure of pep2m makes it an effective probe for studying protein-peptide interactions. It can serve as a bait or competitor in binding assays such as pull-down experiments, surface plasmon resonance, or fluorescence polarization. These applications are critical for mapping interaction motifs, characterizing binding affinities, and elucidating the structural determinants of specificity between peptides and their protein partners. Such studies support the identification of novel regulatory elements and facilitate the rational design of peptide-based modulators.
Enzyme substrate or inhibitor research: In enzymology, pep2m can be utilized as a substrate or competitive inhibitor, depending on its sequence and the target enzyme under investigation. By incorporating the peptide into enzymatic assays, researchers can quantify catalytic activity, determine substrate specificity, or screen for potential inhibitors. This approach is essential for understanding enzyme kinetics, mapping active sites, and developing new strategies for enzyme regulation or inhibition in both basic and applied research contexts.
Peptide synthesis validation: The compound serves as a reference or control in peptide synthesis workflows, particularly during method development and quality assessment. Laboratories may use pep2m to optimize solid-phase peptide synthesis protocols, calibrate analytical instruments such as HPLC or mass spectrometry, and validate purification processes. Its well-defined sequence and physicochemical properties provide a benchmark for assessing synthesis efficiency, purity, and structural integrity in peptide production pipelines.
Cellular uptake and delivery studies: Researchers often employ pep2m to investigate mechanisms of peptide transport, cellular uptake, and intracellular trafficking. By labeling the peptide or modifying it with functional tags, scientists can track its localization and fate within various cell types. These studies are instrumental in evaluating the efficiency of peptide-based delivery systems, understanding membrane translocation processes, and optimizing strategies for intracellular targeting of bioactive compounds or molecular probes.
Blockade of the NSF–GluR2 interaction by a specific peptide (pep2m) introduced into neurons prevented homosynaptic, de novo long-term depression (LTD). Moreover, saturation of LTD prevented the pep2m-induced reduction in AMPAR-mediated excitatory postsynaptic currents (EPSCs). Minimal stimulation experiments indicated that both pep2m action and LTD were due to changes in quantal size and quantal content but were not associated with changes in AMPAR single-channel conductance or EPSC kinetics.
Hippocampal LTD Expression Involves a Pool of AMPARs Regulated by the NSF–GluR2 Interaction
Viral expression of pep2m reduced the surface expression of α-amino-3-hydroxy-5-methyl-isoxazolepropionate (AMPA) receptors, whereas NMDA receptor surface expression in the same living cells was unchanged. In permeabilized neurons, the total amount of GluR2 immunoreactivity was unchanged, and a punctate distribution of GluR2 was observed throughout the dendritic tree.
Surface Expression of AMPA Receptors in Hippocampal Neurons Is Regulated by an NSF-Dependent Mechanism
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