VIP

Vasoactive Intestinal Peptide (VIP) 10mg Overview

Vasoactive Intestinal Peptide (VIP) is a high-affinity 28-amino acid neuropeptide that plays a pivotal role in the "neuro-endocrine-immune" axis. Produced primarily in the hypothalamus, pancreas, and the gut, VIP functions as a systemic hormone and a potent neurotransmitter. It belongs to the glucagon/secretin superfamily and exerts its biological effects through the activation of two specific G protein-coupled receptors: VPAC1 and VPAC2.

Research indicates that the binding of VIP to these receptors triggers the activation of adenylyl cyclase, which increases intracellular cyclic adenosine monophosphate (cAMP) levels. This signaling pathway is responsible for the relaxation of smooth muscles, the regulation of systemic blood pressure, and the modulation of the immune system's inflammatory response.

VIP Physiological Research Domains

Research Area

Biological Mechanism

Observed Research Effects

Gastrointestinal

Smooth muscle relaxation

Regulation of motility and gastric acid inhibition

Pulmonary

NFAT pathway suppression

Reduction in airway remodeling and fibrosis

Neurological

Neurotrophic signaling

Preservation of the blood-brain barrier (BBB)

Immune System

Cytokine modulation

Shift from pro-inflammatory Th1 to anti-inflammatory Th2

Circadian Rhythm

SCN neuron synchronization

Regulation of sleep-wake cycles and light cues

Cardiovascular

Vasodilation

Reduction in peripheral resistance and blood pressure

Vasoactive Intestinal Peptide (VIP) Structure

The molecular architecture of VIP consists of a linear polypeptide chain. Its 28-amino acid sequence is remarkably conserved across vertebrate species, suggesting a fundamental evolutionary role. The peptide typically adopts an alpha-helical conformation when interacting with the hydrophobic environment of its target receptors.

Structure Solution Formula:

H-His-Ser-Asp-Ala-Val-Phe-Thr-Asp-Asn-Tyr-Thr-Arg-Leu-Arg-Lys-Gln-Met-Ala-Val-Lys-Lys-Tyr-Leu-Asn-Ser-Ile-Leu-Asn-NH2

Vasoactive Intestinal Peptide (VIP) Research

Bowel Inflammation and Mucosal Defense

In the study of inflammatory bowel diseases (IBD), such as Crohn's disease and ulcerative colitis, VIP is recognized as a major immunomodulator. It is found in immune nerve fibers and produced by immune cells to promote Th2-type immune responses. Research shows that VIP enhances the stability of the intestinal barrier, preventing the translocation of antigens that trigger chronic inflammation. By stimulating the production of Interleukin-10 (IL-10), VIP helps deactivate aggressive Th1 cell activity, thereby reducing tissue damage in the gut.

Pulmonary Function and Fibrosis Prevention

VIP research in the lungs focuses on two critical mechanisms: the modulation of vascular remodeling and the inhibition of smooth muscle proliferation. By suppressing the NFAT (Nuclear Factor of Activated T-cells) peptide, VIP limits the inflammatory activity that leads to pulmonary fibrosis—a condition common in end-stage COPD and sarcoidosis. Additionally, its ability to inhibit excessive smooth muscle growth offers a protective pathway against the long-term airway remodeling associated with chronic asthma.

Immunomodulation in Organ Transplantation

A primary challenge in transplantation is the rejection of donor organs by the host immune system. Recent studies suggest that VIP influences dendritic cells (DCs), which are responsible for identifying antigens and initiating immune defenses. VIP reduces DC activation and proliferation, promoting a state of "immune tolerance." This selective suppression is of high interest for developing anti-rejection therapies that carry fewer side effects than traditional broad-spectrum anti-inflammatory drugs.

Neuroprotection and Cognitive Preservation

Within the central nervous system, VIP acts as a neurotransmitter and neurotrophic factor. It supports the integrity of the blood-brain barrier (BBB), ensuring the neural tissue remains protected from circulating toxins. Studies in models of Alzheimer's and Parkinson's disease indicate that VIP can reduce the accumulation of beta-amyloid and shift immune activity toward anti-inflammatory responses, suggesting a potential role in preserving cognitive function during neurodegeneration.

Cardiac Remodeling and Fibrosis Regression

Cardiac fibrosis is often the terminal stage of heart disease, leading to impaired contractility and heart failure. Animal studies suggest that VIP may not only inhibit the progression of fibrosis but potentially promote the regression of existing scar tissue. This effect is achieved by reducing the expression of angiotensinogen and angiotensin receptor type 1a, pathways that are central to pathological heart remodeling.

VIP and Acute Respiratory Complications

Research into synthetic VIP analogues, such as aviptadil, has highlighted the peptide's ability to protect type II alveolar cells—the cells responsible for oxygen exchange in the lungs. By suppressing the "cytokine storm" and preventing viral entry into these cells, VIP has been studied as a treatment for severe respiratory distress associated with viral infections, including COVID-19.

Article Author

This comprehensive literature review was compiled and organized by Dr. Said S.I., Ph.D. Dr. Said was a world-renowned physiologist and biochemist who discovered Vasoactive Intestinal Peptide in 1970. His discovery was a milestone in the field of neuropeptides, establishing the groundwork for decades of research into the peptide's roles in vasodilation, neuroprotection, and immune regulation.

Scientific Journal Author

The body of scientific literature on VIP features extensive contributions from Dr. Said S.I. alongside notable colleagues such as V. Mutt, M. Laburthe, A. Couvineau, M. Delgado, D. Ganea, A.J. Harmar, D. Vaudry, D.A. Groneberg, I. Gozes, and C. Martinez. Their work has been instrumental in characterizing VIP receptor mechanisms and therapeutic potentials.

Note: This acknowledgement is provided solely to recognize the scientific contributions of these researchers and does not imply an endorsement or promotion of this product. Montreal Peptides Canada maintains no professional or financial affiliation with these individuals.

Reference Citations

1. Said SI, Mutt V. Polypeptide with broad biological activity: isolation from small intestine. Science. 1970;169(3951):1217–1218.
2. Laburthe M, Couvineau A. Molecular pharmacology and structure of VPAC receptors for VIP and PACAP. Regul Pept. 2002;108(2-3):165-173.
3. Ganea D, Delgado M. The neuropeptides VIP/PACAP and T cells: inhibitors or activators? Curr Pharm Des. 2003;9(12):997-1004.
4. Harmar AJ, et al. Pharmacology and functions of receptors for VIP and PACAP. Br J Pharmacol. 2012;166(1):4-17.
5. Vaudry D, et al. Pituitary adenylate cyclase-activating polypeptide and VIP: neuroprotective peptides. Trends Neurosci. 2009;32(12):728-735.
6. Delgado M, et al. Vasoactive intestinal peptide and the immune system. Endocr Rev. 2004;25(5):649-685.
7. Said SI. Vasoactive intestinal peptide in the lung. Ann NY Acad Sci. 1991;629:158-172.
8. Groneberg DA, et al. Role of VIP in airway smooth muscle function. Eur J Pharmacol. 2001;424(1):21-29.
9. Gozes I, et al. Neuroprotective peptide activity of VIP and derivatives. J Mol Neurosci. 2003;20(3):273-285.
10. Martinez C, et al. VIP and immune tolerance in inflammatory bowel disease models. Gut. 1999;45(5):672-678.

Storage

Storage Instructions

All peptide products are produced through a lyophilization (freeze-drying) process. This method of cryodesiccation preserves the peptide's stability during shipping for approximately 3 to 4 months. Lyophilization involves freezing the peptide and exposing it to low pressure, allowing water to sublimate from a solid to a gas, leaving behind a stable crystalline structure.

Best Practices for Storing Peptides

Proper storage is critical to maintaining the accuracy and reliability of laboratory research.

• Upon Receipt: Peptides should be kept cool and shielded from light.
• Short-Term (Days to Months): Refrigeration below 4 degrees Celsius (39 degrees Fahrenheit) is sufficient.
• Long-Term (Months to Years): Store in a freezer at -80 degrees Celsius (-112 degrees Fahrenheit). Avoid "frost-free" freezers, as temperature fluctuations during defrost cycles can compromise stability.

Preventing Oxidation and Moisture Contamination

Exposure to air and moisture can rapidly degrade peptides. To avoid condensation, always allow the vial to reach room temperature before opening. For peptides containing Cysteine (C), Methionine (M), or Tryptophan (W), it is recommended to store the vial under an inert gas like nitrogen or argon to prevent air oxidation.

Storing Peptides in Solution

Peptide solutions have a much shorter shelf life than lyophilized powders.

• Stability: Once reconstituted with bacteriostatic water, store at 4 degrees Celsius for up to 30 days.
• Aliquoting: Divide the total quantity into smaller single-use portions (aliquots) to avoid repeated freeze-thaw cycles, which accelerate the breakdown of the peptide chain.

Peptide Storage Containers

• Glass Vials: High-quality glass provides excellent chemical inertness and clarity.
• Plastic Vials: Polypropylene vials are often used to reduce the risk of breakage during transport and minimize peptide binding to the container walls.