Vasonatrin peptide (VNP) is a chimera of atrial natriuretic peptide (ANP) and C-type natriuretic peptide (CNP) with potent venodilating and natriuretic activity.
CAT No: R1748
Vasonatrin Peptide VNP is a synthetic peptide compound recognized for its unique hybrid structure, which combines functional motifs from both atrial natriuretic peptide (ANP) and C-type natriuretic peptide (CNP). Structurally designed to emulate and extend the biological activities of its parent peptides, VNP has garnered significant interest in cardiovascular and renal research due to its potent natriuretic, diuretic, and vasorelaxant properties. Its ability to modulate vascular tone and fluid homeostasis makes it a valuable biochemical tool for investigating natriuretic peptide signaling pathways and their physiological implications. As a research-use peptide, VNP enables precise exploration of receptor selectivity, downstream signaling mechanisms, and the broader pharmacodynamics of natriuretic peptides in experimental settings.
Peptide receptor pharmacology: Vasonatrin Peptide VNP serves as a critical probe in studies aimed at delineating the receptor specificity and pharmacological profiles of natriuretic peptides. By virtue of its chimeric sequence, VNP interacts with both NPR-A and NPR-B receptors, offering researchers a means to dissect receptor-mediated signaling events in vascular smooth muscle cells and renal tissues. This application is particularly relevant for elucidating the cross-talk between different natriuretic peptide receptors and understanding their roles in regulating blood pressure and extracellular fluid balance.
Vascular biology research: The peptide's robust vasorelaxant activity positions it as a powerful agent for investigating endothelial function and vascular reactivity. In isolated vessel assays and organ bath experiments, VNP is frequently employed to assess mechanisms underlying smooth muscle relaxation, endothelial nitric oxide synthesis, and the modulation of vascular tone. Such studies contribute to a deeper understanding of cardiovascular homeostasis and the molecular basis of vasodilation, supporting the development of novel strategies for managing vascular dysfunction in preclinical models.
Renal physiology studies: Vasonatrin Peptide VNP is widely utilized in experimental models to explore renal hemodynamics, glomerular filtration, and the regulation of sodium and water excretion. Its natriuretic and diuretic effects provide a foundation for investigating the integration of peptide signaling within the kidney, including the modulation of tubular transport processes and the interplay with other hormonal systems. These applications are essential for advancing knowledge of renal adaptive responses and fluid-electrolyte homeostasis under physiological and pathophysiological conditions.
Peptide structure-function analysis: The hybrid nature of VNP offers unique opportunities for structure-activity relationship (SAR) studies in peptide chemistry. By comparing the biological activities of VNP with those of its parent peptides, researchers can identify critical sequence determinants responsible for receptor binding, activation, and downstream effects. Such comparative analyses inform the rational design of next-generation natriuretic peptide analogs with tailored pharmacological properties, thereby supporting innovation in peptide engineering and synthetic biology.
Peptide assay development: Vasonatrin Peptide VNP is also employed as a reference standard or functional control in the development and validation of bioassays designed to quantify natriuretic peptide activity. Its well-characterized profile enables the calibration of in vitro and ex vivo systems that monitor cyclic GMP production, receptor activation, or cellular responses to natriuretic peptides. These assay systems are invaluable for screening novel peptide analogs, evaluating receptor agonists or antagonists, and conducting high-throughput studies that advance peptide-based research and drug discovery.
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