A cyclic peptide that disrupts interaction between GluK2 (formally GluR6) and postsynaptic density protein 95 (PSD-95) through competing with the C terminal of GluK2 to bind the PDZ1 domain of PSD-95. It inhibits clustering of kainate receptors.
CAT No: R0842
CAS No:1315378-73-4
Synonyms/Alias:PDZ1 Domain inhibitor peptide;1315378-73-4;(2S)-2-[[(2S)-2-[[(2S,5S,14S)-14-[[(2S)-6-amino-2-[[(2S)-2-amino-3-(4-hydroxyphenyl)propanoyl]amino]hexanoyl]amino]-2-[(1R)-1-hydroxyethyl]-3,8,15-trioxo-1,4,9-triazacyclopentadecane-5-carbonyl]amino]propanoyl]amino]-3-methylbutanoic acid;PDZ1 Domain inhibitor peptide TFA;HY-P1195;AKOS024456989;AS-85550;DA-76677;PD070684;CS-0028949;G17881;S-1315378-73-4;
PDZ1 Domain inhibitor peptide is a specialized synthetic peptide designed to selectively disrupt protein-protein interactions mediated by the PDZ1 domain, a modular protein interaction motif found in many signaling and scaffolding proteins. By mimicking or competitively binding to the PDZ1 domain, this peptide serves as a powerful molecular tool for probing the biochemical and structural roles of PDZ-mediated complexes in cellular signaling pathways. Its application has become increasingly significant in elucidating the spatial and temporal dynamics of synaptic organization, signal transduction, and membrane protein trafficking, making it highly relevant for researchers investigating the molecular underpinnings of cell communication and organization.
Protein-protein interaction studies: The inhibitor peptide is widely utilized in mechanistic studies to dissect the specific contributions of PDZ1 domain-mediated interactions within multi-protein complexes. By competitively blocking endogenous binding partners, researchers can selectively impair the assembly or stability of protein networks, thereby revealing the functional impact of individual PDZ1-mediated contacts. This approach is invaluable for characterizing the specificity and affinity of PDZ1 interactions and for mapping the interaction landscape within complex signaling pathways.
Signal transduction research: Disruption of PDZ1 domain interactions using this peptide enables precise interrogation of signaling cascades involving PDZ-containing scaffold proteins. Such scaffolds are pivotal for organizing kinases, phosphatases, and other signaling molecules at defined cellular locations. Application of the inhibitor peptide facilitates the study of how perturbing these interactions alters downstream signaling events, allowing for detailed analysis of pathway regulation, cross-talk, and feedback mechanisms in diverse cellular contexts.
Synaptic biology and neurobiology: In the context of neuronal research, the peptide is frequently employed to investigate the molecular determinants of synaptic assembly, maintenance, and plasticity. PDZ1 domains are integral to the postsynaptic density and are involved in clustering neurotransmitter receptors and associated signaling proteins. By selectively inhibiting these interactions, scientists can examine the consequences for synaptic strength, receptor localization, and neuronal communication, providing insights into the molecular basis of learning, memory, and neurodevelopmental processes.
Membrane protein trafficking: The inhibitor peptide is a valuable tool for studying the intracellular trafficking and surface expression of membrane proteins that rely on PDZ1 domain interactions for proper localization. Disrupting these interactions can reveal mechanisms governing the sorting, recycling, or degradation of channels, transporters, and receptors, thereby advancing understanding of membrane dynamics and protein turnover in physiological and pathophysiological states.
Peptide-based assay development: In addition to its functional applications, the PDZ1 Domain inhibitor peptide serves as a reference molecule or competitive ligand in the development and optimization of binding assays. Its defined specificity for the PDZ1 domain enables its use in fluorescence polarization, surface plasmon resonance, or pull-down assays aimed at quantifying binding affinities, screening for novel inhibitors, or validating the selectivity of small-molecule modulators. This supports both basic research and high-throughput screening initiatives focused on targeting PDZ1-mediated interactions.
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