Targefrin presents a peptide-derived framework designed to interrogate receptor-recognition motifs and epitope architecture. Hydrophobic and charged residues cooperate to define binding surfaces and solubility. Researchers monitor its conformational states in aqueous and membrane-like environments. Applications include ligand-screening panels, peptide-optimization campaigns, and structure-function investigations.
CAT No: R2848
Synonyms/Alias:Targefrin; CHEMBL5192123; EphA2 degrader 27; GLXC-26516; HY-P3717; BDBM50588608; 3031514-44-7; (Piperazin-1-yl)Ac-(4-NH2)Phe-Leu-Ala-(4-(2-CF3)phenyl)Phe-Pro-Asp-Ala-Chg-Pro-Phe-Arg-Pro-NH2
Targefrin is a synthetic peptide compound designed to interact specifically with the epidermal growth factor receptor (EGFR), a transmembrane protein that plays a pivotal role in cellular signaling pathways associated with proliferation, differentiation, and survival. As a targeted peptide ligand, Targefrin is structurally optimized to bind with high affinity to the extracellular domain of EGFR, making it a valuable molecular tool for dissecting receptor-mediated processes in cellular models. Its defined sequence and selective binding characteristics position it as a crucial reagent in studies aiming to elucidate EGFR-driven mechanisms, assess receptor function, and develop innovative approaches in receptor-targeted research.
Receptor binding studies: Targefrin is extensively employed in receptor binding assays to characterize the affinity, specificity, and kinetics of ligand-EGFR interactions. By using radiolabeled or fluorescently tagged versions of the peptide, researchers can quantitatively assess binding parameters and compare the efficacy of competitive ligands or inhibitors. Such studies are fundamental for mapping the ligand-binding site, identifying conformational changes upon binding, and understanding the molecular determinants of receptor activation or inhibition.
Signal transduction research: The peptide's selective engagement with EGFR enables detailed investigation of downstream signaling cascades, including MAPK, PI3K/AKT, and STAT pathways. By introducing Targefrin to cultured cells or membrane preparations, scientists can monitor phosphorylation events, protein-protein interactions, and transcriptional responses triggered by receptor activation. This approach supports the delineation of pathway-specific effects, cross-talk with other receptors, and the identification of novel regulatory nodes within EGFR-mediated signaling networks.
Cellular imaging and localization: Fluorescently labeled Targefrin provides a powerful tool for visualizing EGFR distribution, trafficking, and internalization dynamics in live or fixed cells. Through confocal microscopy or flow cytometry, the peptide facilitates real-time tracking of receptor movement, endocytosis, and recycling processes. Such imaging applications are instrumental in exploring spatial aspects of receptor biology, assessing the impact of microenvironmental factors, and evaluating the effects of pharmacological modulators on receptor localization.
Peptide-based screening platforms: Targefrin serves as a functional component in high-throughput screening assays designed to identify novel EGFR modulators, antagonists, or allosteric effectors. By incorporating the peptide into binding or competition assays, researchers can rapidly evaluate compound libraries for their ability to modulate receptor-ligand interactions. This application accelerates the discovery of new chemical entities with potential utility in research and development settings focused on receptor biology.
Targeted delivery studies: The high specificity of Targefrin for EGFR makes it an attractive vector for targeted delivery of molecular probes, nanoparticles, or other conjugated payloads to EGFR-expressing cells. By coupling the peptide to various cargoes, researchers can investigate cell-specific uptake, intracellular trafficking, and the efficiency of targeted delivery strategies. Such studies contribute to the optimization of ligand-mediated targeting approaches for in vitro and in vivo experimental models, advancing the field of receptor-directed molecular engineering.
2. Cell-based adhesion assays for isolation of snake venom’s integrin antagonists
4. Implications of ligand-receptor binding kinetics on GLP-1R signalling
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