xStAx-VHLL is a stapled α-helical peptide designed to stabilize hydrophobic and charged residues in a rigid conformation. The staple enforces helical geometry and enhances proteolytic resistance. Researchers examine its PPI-inhibitor potential and conformational behavior. Applications include helix-mimetic development, structural biophysics, and ligand optimization.
CAT No: R2838
Synonyms/Alias:xStAx-VHLL;β-catenin degrader xStAx-VHLL; GLXC-25272
xStAx-VHLL is a synthetic peptide compound engineered for advanced biochemical research applications. As a member of the xStAx (extended stapled alpha-helix) peptide family, it features a hydrocarbon-stapled structure designed to stabilize alpha-helical conformations and enhance proteolytic resistance. The incorporation of the VHLL motif within its sequence enables targeted interactions with specific protein domains, making it highly relevant to studies of protein-protein interactions, intracellular signaling, and molecular recognition. Its unique conformational rigidity and enhanced cell permeability distinguish it as a valuable tool for probing complex biological systems and for the development of next-generation research reagents.
Protein-Protein Interaction Studies: xStAx-VHLL is widely employed in the investigation of protein-protein interactions, particularly those involving alpha-helical recognition motifs. The hydrocarbon-stapled configuration confers enhanced structural stability, allowing researchers to dissect transient or weak interactions that are otherwise challenging to study using linear peptides. By mimicking endogenous alpha-helical segments, it serves as a robust probe for mapping binding interfaces and elucidating the molecular determinants of specificity in multi-protein complexes.
Cell Penetration and Intracellular Delivery: The stapled peptide architecture of xStAx-VHLL provides improved cell permeability compared to conventional peptides. This property is leveraged in studies requiring efficient intracellular delivery of bioactive sequences, enabling the modulation of signaling pathways or the inhibition of specific protein interactions within live cells. Its ability to traverse cellular membranes without significant degradation makes it a preferred scaffold for functional assays in cell-based experimental systems.
Structural Biology and Conformational Analysis: Researchers utilize xStAx-VHLL as a model system for exploring alpha-helical stabilization and conformational dynamics. The hydrocarbon staple restricts backbone flexibility, facilitating high-resolution structural studies via NMR spectroscopy or X-ray crystallography. These insights are instrumental for understanding the principles governing peptide folding, helix stabilization, and the design of conformationally constrained biomolecules for research applications.
Peptide Engineering and Design Validation: The compound serves as an exemplary template for validating peptide engineering strategies aimed at enhancing biological activity and stability. Its sequence and stapling pattern can be systematically modified to assess the impact of structural alterations on binding affinity, specificity, and resistance to proteolysis. Such studies inform the rational design of next-generation peptides for use in biochemical assays, molecular probes, or as scaffolds for further functionalization.
Assay Development and Screening: xStAx-VHLL is incorporated into a variety of in vitro and cell-based assay formats, supporting the development of platforms for high-throughput screening of modulators targeting protein-protein interfaces. Its defined biophysical properties and robust performance facilitate the establishment of reproducible, sensitive assays for the identification and characterization of small molecules, peptides, or other interactors that influence biologically relevant signaling pathways.
3. The spatiotemporal control of signalling and trafficking of the GLP-1R
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