EphA4 receptor tyrosine kinase inhibitor (Kd = 0.8 μM), which inhibits EphA4-EphrinA5 interactions (IC50 = 6.34 μM), prevents AβO induced synaptic damage, dendritic spine loss and prevents the blocking of LTP in hippocampal CA3-CA1 transmissions. It shows neuroprotective effect.
CAT No: R0975
CAS No:676657-00-4
Synonyms/Alias:676657-00-4;KYL peptide;L-Leucine,L-lysyl-L-tyrosyl-L-leucyl-L-prolyl-L-tyrosyl-L-tryptophyl-L-prolyl-L-valyl-L-leucyl-L-seryl-L-seryl-;KYL (trifluoroacetate salt);KYL;KYL TFA;HY-P2264;AKOS025142078;DA-54717;CS-0120761;G15846;
KYL is a synthetic peptide compound recognized for its unique amino acid sequence and functional properties, making it a valuable tool in biochemical and molecular research. As a member of the peptide class, KYL is designed to interact with specific protein targets or cellular receptors, facilitating the study of signaling pathways and molecular mechanisms in vitro. Its sequence and structural features enable targeted investigations into protein-protein interactions, receptor modulation, and peptide-based assay development. Researchers utilize KYL to probe the intricacies of cell signaling, protein functionality, and as a reference compound in various experimental systems, underscoring its significance in advancing peptide science.
Receptor binding studies: KYL is frequently employed to investigate the binding dynamics and specificity of peptide-receptor interactions. Its sequence is tailored to engage with particular cell surface receptors, allowing researchers to characterize ligand affinity, receptor occupancy, and downstream signal transduction events. By using KYL in binding assays, scientists can delineate the molecular determinants of receptor recognition, contributing to a deeper understanding of cellular communication and the modulation of signaling networks.
Peptide structure-activity relationship (SAR) analysis: The compound serves as a model peptide for systematic SAR investigations, where modifications to its amino acid residues or terminal groups can elucidate the relationship between peptide structure and biological activity. Through such studies, KYL provides critical insights into the functional domains responsible for activity, guiding the rational design of novel peptide analogs with enhanced specificity or potency for research applications.
Cellular signaling pathway elucidation: KYL is utilized in cell-based assays to dissect the activation or inhibition of specific intracellular signaling cascades. By introducing the peptide to cultured cells, researchers can monitor changes in phosphorylation patterns, gene expression profiles, or other downstream effects, thereby mapping the molecular pathways influenced by peptide-receptor engagement. This application is especially valuable in the context of identifying key regulatory nodes and potential targets for further biochemical investigation.
Peptide synthesis optimization: Beyond its biological applications, KYL is also used as a reference sequence in the optimization of solid-phase peptide synthesis protocols. Its defined length and sequence complexity provide an ideal template for evaluating coupling efficiencies, protecting group strategies, and purification methods. By benchmarking synthetic outcomes with KYL, peptide chemists can refine methodologies to improve yield, purity, and reproducibility in the production of research-grade peptides.
Analytical method development: The well-characterized nature of KYL makes it suitable for validating and calibrating analytical techniques such as high-performance liquid chromatography (HPLC), mass spectrometry, and capillary electrophoresis. Laboratories incorporate KYL as a standard to assess instrument performance, method sensitivity, and quantification accuracy, ensuring robust and reliable analysis of peptide samples in diverse research settings.
KYL was also shown to prevent growth cone collapse in chicken retinal explants and dissociated cultures of rat cortical neurons, promote nerve regeneration and functional recovery in a rat model of spinal cord injury, and inhibit the adhesion of human T-cells to endothelial cells. Thus, KYL can target human, mouse, rat and chicken EphA4 and may be useful for promoting nerve regeneration after injury and modulating immune responses.
Distinctive Binding of Three Antagonistic Peptides to the Ephrin-Binding Pocket of the EphA4 Receptor
STI and KYL inhibitors prevented AβO-induced dendritic spine loss. Although the absence of EphA4 did not completely rescue the dendritic spine loss, EphA4-knockout neurons show a significant decrease in AβO-induced dendritic spine loss. Furthermore, protection was observed in mature neurons (with established synapses) transfected with either c-Abl shRNA or EphA4 shRNA.
EphA4 activation of c-Abl mediates synaptic loss and LTP blockade caused by amyloid-β oligomers
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