VIP(6-28)(human, rat, porcine, bovine) is an effective antagonist of the actions of exogenous vasoactive intestinal peptide (VIP) on cAMP.
VIP(6-28)(human, rat, porcine, bovine) is a synthetic peptide fragment derived from vasoactive intestinal peptide (VIP), corresponding to amino acid residues 6 through 28 of the native sequence. As a truncated analog, it is recognized for its role as a potent antagonist of VIP receptors, particularly the VPAC1 and VPAC2 subtypes. By selectively inhibiting the biological actions of endogenous VIP, this peptide has become an invaluable tool in neurobiology, immunology, and receptor pharmacology research. Its cross-species sequence compatibility with human, rat, porcine, and bovine systems further enhances its relevance for comparative studies and translational peptide research.
Receptor Antagonism Studies: VIP(6-28) is widely employed as a selective antagonist in investigations of VIP receptor-mediated signaling pathways. By competitively binding to VPAC1 and VPAC2 receptors without eliciting agonist activity, it enables researchers to delineate the specific physiological and cellular responses attributable to endogenous VIP. This approach is instrumental in dissecting the contribution of VIP signaling to processes such as smooth muscle relaxation, neurotransmission, and endocrine regulation across various tissue types.
Neurobiology Research: In the context of central and peripheral nervous system studies, VIP(6-28) serves as an essential probe for elucidating the modulatory effects of VIP on neuronal excitability, synaptic plasticity, and neuropeptide release. Its use allows for the selective inhibition of VIP-driven mechanisms, facilitating the investigation of neural circuits involved in circadian rhythm regulation, neuroprotection, and neuroinflammation. Such studies provide critical insights into the complex interplay between neuropeptides and neuronal function.
Immunological Investigations: The peptide is frequently utilized to explore the immunoregulatory roles of VIP, particularly in models of inflammation and immune cell signaling. By blocking VIP activity, researchers can assess its impact on cytokine production, lymphocyte proliferation, and immune cell trafficking. This application aids in clarifying the mechanisms by which VIP modulates innate and adaptive immune responses, thereby advancing the understanding of neuroimmune communication.
Peptide Structure-Activity Relationship Analysis: VIP(6-28) is an important tool for structure-activity relationship (SAR) studies aimed at mapping the functional domains of VIP necessary for receptor interaction and biological activity. Truncation and modification experiments using this fragment help identify critical residues involved in receptor binding and signal transduction, guiding the rational design of novel peptide analogs with tailored pharmacological profiles.
Comparative Species Studies: Owing to its sequence conservation across human, rat, porcine, and bovine species, VIP(6-28) is particularly useful in comparative studies that investigate interspecies differences and similarities in VIP receptor pharmacology. This enables the assessment of evolutionary conservation of peptide-receptor interactions and supports translational research models where findings in animal systems can inform human biology. Such cross-species analyses are essential for validating experimental outcomes and advancing peptide-based research initiatives.
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