Super-TDU (1-31) is a peptide of Super-TDU, which is an inhibitor of YAP-TEADs, shows potent anti-tumor activity.
CAT No: R1696
Super-TDU 1-31 is a synthetic peptide fragment derived from the Dishevelled (Dvl) protein, specifically corresponding to the first 31 amino acids of the TDU (Thr-Asp-U) region. As a functionally significant peptide in the context of Wnt/β-catenin signaling, Super-TDU 1-31 is widely utilized in biochemical research to dissect protein-protein interactions and investigate intracellular signaling mechanisms. Its defined sequence enables precise modulation of Dishevelled-mediated pathways, making it a valuable molecular tool for elucidating the roles of Dvl in cellular communication, developmental biology, and disease modeling. The peptide's utility extends to studies focusing on the structural and functional domains of signaling proteins, supporting advanced research in cell signaling and molecular biology.
Signal Transduction Research: Super-TDU 1-31 is extensively employed in studies exploring Wnt/β-catenin signaling, a pathway integral to embryogenesis, cell differentiation, and tissue homeostasis. By mimicking the native TDU motif of Dishevelled, the peptide serves as a competitive inhibitor or probe to analyze the recruitment and assembly of key signaling complexes. Researchers utilize it to dissect the molecular determinants governing pathway activation, providing insights into the modulation of signal transduction networks and the consequences of aberrant pathway regulation in developmental and pathological contexts.
Protein-Protein Interaction Studies: The peptide's defined sequence allows it to function as a molecular probe in mapping interactions between the Dishevelled protein and its binding partners. In vitro and cell-based assays often employ Super-TDU 1-31 to characterize the specificity and affinity of TDU-mediated contacts, aiding in the identification of novel interaction motifs and regulatory elements. This application is critical for unraveling the mechanisms by which Dishevelled orchestrates downstream signaling events and for validating potential targets in pathway modulation.
Peptide-Based Inhibitor Development: Super-TDU 1-31 provides a template for the rational design and screening of peptide inhibitors targeting the Dvl TDU domain. Its use in structure-activity relationship (SAR) studies enables researchers to optimize sequence modifications for enhanced binding or inhibitory properties. Such efforts are central to the development of molecular tools that can modulate Dishevelled function with high specificity, supporting both basic research and the exploration of novel chemical biology strategies.
Structural Biology and Biophysical Analysis: The well-characterized nature of Super-TDU 1-31 makes it suitable for structural and biophysical investigations, including NMR spectroscopy, X-ray crystallography, and surface plasmon resonance (SPR). Researchers utilize the peptide to elucidate the conformational dynamics of the TDU region, assess binding interfaces, and quantify interaction kinetics with effector proteins. These studies contribute to a deeper understanding of the structural basis for Dishevelled-mediated signaling and inform the rational design of modulators for pathway intervention.
Cellular Functional Assays: In cell-based experimental systems, Super-TDU 1-31 is applied to modulate endogenous signaling events, enabling functional analysis of Dishevelled activity in living cells. By introducing the peptide into cultured cells, researchers can monitor downstream transcriptional responses, cytoskeletal rearrangements, or other phenotypic outcomes associated with Wnt pathway perturbation. These assays provide a dynamic platform for evaluating the biological consequences of TDU-mediated interactions and for validating mechanistic hypotheses in a physiologically relevant context.
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