VIR-165 is a modified form of virus inhibitory peptide (VIRIP) that binds the fusion peptide of the gp41 subunit and prevents its insertion into the target membrane. VIRIP inhibits a wide variety of human immunodeficiency virus type 1 (HIV-1) strains.
CAT No: R1750
VIR-165 is a synthetic peptide compound specifically designed for advanced biochemical research applications. As a peptide, it consists of a defined sequence of amino acids, conferring unique structural and functional properties that make it valuable in studies involving protein-protein interactions, molecular recognition, and cellular signaling pathways. Its sequence and conformation allow for precise investigation of peptide-mediated biological processes, positioning it as a critical tool in the exploration of molecular mechanisms underlying various physiological and pathological events. The robust design and versatility of VIR-165 enable researchers to dissect complex biochemical systems with high specificity and reproducibility.
Peptide interaction studies: VIR-165 serves as a powerful probe for dissecting protein-peptide and peptide-peptide interactions. By introducing this sequence into binding assays or structural studies, researchers can map interaction interfaces, determine binding affinities, and elucidate the molecular determinants that govern specificity. Such insights are instrumental for understanding the assembly of multiprotein complexes, signaling cascades, and regulatory networks in cellular environments.
Peptide synthesis and optimization: The defined structure of VIR-165 makes it an ideal reference or template in peptide synthesis workflows. It can be utilized to benchmark synthetic methodologies, validate purification protocols, and optimize conditions for solid-phase peptide synthesis (SPPS). Its application in synthesis development supports the generation of high-quality peptides with consistent yield and sequence fidelity, which is essential for downstream research applications and the creation of peptide libraries.
Functional assays and mechanistic studies: Researchers frequently employ VIR-165 in functional assays to investigate the biological activity of peptide sequences within cellular or cell-free systems. By integrating this peptide into biochemical assays, it is possible to monitor its effects on enzymatic activity, signal transduction, or cellular responses. Such studies provide valuable mechanistic insights into how specific peptide motifs modulate biological processes and contribute to the regulation of cellular functions.
Structural biology applications: The unique sequence of VIR-165 makes it suitable for structural characterization using techniques such as NMR spectroscopy, X-ray crystallography, or cryo-electron microscopy. Structural studies involving this peptide can reveal conformational dynamics, secondary structure preferences, and intermolecular contacts. These data inform the rational design of peptide analogs with enhanced stability or biological properties and support the broader field of peptide-based structural biology.
Peptide-based inhibitor development: As a well-characterized synthetic peptide, VIR-165 can be employed as a starting scaffold for the development of peptide-based inhibitors targeting specific protein interactions or enzymatic activities. By systematically altering its sequence or chemical modifications, scientists can generate analogs with improved binding properties or selectivity. This approach is central to the discovery of research tools that modulate biological pathways, facilitating target validation and mechanistic exploration in preclinical research settings.
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