pe
pep-10468 v1 CC-BY-SA-4.0

VIP: Vasoactive Intestinal Peptide, natural nerve-and-immune messenger

A natural signaling peptide made throughout the body, in the gut, lungs, brain, and immune system, that relaxes smooth muscle, calms inflammation, and helps maintain nerve cells; used as a lab research tool.

statusbioassayed targetVPAC1 length28 aa refs9
status 5 / 5
prediction metrics boltz-2 2.2.1
ipTM0.873
pTM0.842
avg pLDDT53.1
ranking score0.599
STRUCTURE · PEP-10468 × VPAC1
ranking0.599
target interface 4.5Å peptide drag rotate · ctrl+scroll zoom · right-click pan
boltz-2 2.2.1 · mmCIF ↓ download
sequence28 aa
151015202528
HSDAVFTDNYTRLR KQMAVKKYLNSILN
overview readme

What this is

Vasoactive Intestinal Peptide (VIP) is a 28-amino acid neuropeptide found throughout the body — in the gut, lungs, brain, and immune system. It is an endogenous signaling molecule, not a synthetic drug: the body produces it continuously, and it plays broad regulatory roles in smooth-muscle tone, immune balance, and nerve-cell maintenance. The peptide was first isolated from porcine intestinal extracts in the early 1970s by Sami Said and Viktor Mutt at the Karolinska Institute, initially characterized as a potent vasodilator. The stored sequence (HSDAVFTDNYTRLRKQMAVKKYLNSILN) represents the linear backbone; the biologically active form carries a C-terminal amide (–NH₂) not shown in the raw sequence, which protects the peptide from carboxypeptidase degradation and is required for full receptor binding.

Despite an attractive pharmacological profile, VIP has never reached routine clinical use as an approved drug. Its very short plasma half-life (under one minute in circulation, per Iwasaki and colleagues, F1000Research 2019), broad receptor distribution, and vasodilatory effects at pharmacologic doses have made therapeutic development difficult. A synthetic form, aviptadil, was investigated extensively for COVID-19-related acute respiratory distress syndrome and pulmonary hypertension; the FDA declined an Emergency Use Authorization for intravenous aviptadil in 2021. VIP is also used in the Shoemaker CIRS (Chronic Inflammatory Response Syndrome) protocol as an off-label intranasal therapy, though that indication lacks large-RCT support and the CIRS diagnostic framework is not accepted by mainstream medicine.

History

VIP was isolated in 1970 from porcine intestinal extracts by Sami Said and Viktor Mutt at the Karolinska Institute, first characterized as a potent vasodilator — which is how it got its name. Over subsequent decades its biology expanded well beyond vascular tone: the peptide was found distributed throughout the central and peripheral nervous systems, immune compartments, and endocrine tissues. By the 1980s it was recognized as a neurotransmitter candidate in nonadrenergic, noncholinergic (NANC) inhibitory innervation, and subsequently its roles in circadian regulation through the suprachiasmatic nucleus and in neuroprotection through the activity-dependent neuroprotective protein (ADNP) pathway were characterized in the literature.

The two receptor subtypes — VPAC1 and VPAC2 — were cloned and characterized as class B GPCRs, and their molecular pharmacology including accessory protein interactions was reviewed by Couvineau and colleagues (British Journal of Pharmacology, 2012). A cryo-EM structure of the human VIP1 receptor in complex with PACAP27 and a Gs heterotrimer was resolved in 2020, providing the first detailed structural picture of ligand engagement (Duan and colleagues, Nature Communications, 2020).

In the 2010s, aviptadil — a pharmaceutical-grade synthetic VIP — was advanced by Relief Therapeutics and NeuroRx for ARDS and pulmonary hypertension, becoming a high-profile investigational therapy during the COVID-19 pandemic. The FDA declined EUA for IV aviptadil in 2021, and the TESICO randomized controlled trial of IV aviptadil plus remdesivir versus placebo did not support clear efficacy in COVID-19 hypoxaemic respiratory failure. Research into VIP for autoimmune diseases including rheumatoid arthritis, lupus, and Graves' disease has continued in parallel.

What it does

VIP acts as a natural anti-inflammatory messenger and smooth-muscle relaxant. In the lungs, it dilates blood vessels and relaxes airway smooth muscle — the property that drove its investigation in pulmonary hypertension and respiratory failure. In the immune system, it shifts the balance away from inflammatory signaling, reducing the output of pro-inflammatory signals and promoting immune-regulatory cell types. In the nervous system, it supports neuron survival and modulates brain-clock timing via the suprachiasmatic nucleus.

The peptide also regulates gut function: it influences ion secretion, smooth-muscle motility, and mucosal immune responses. Iwasaki and colleagues (F1000Research, 2019) reviewed VIP's physiological and pathological roles in the gastrointestinal system, noting effects on circadian rhythms and glycemic control in addition to its classical gut-motility actions.

Evidence

  • Human: Moderate. Multiple randomized controlled trials of aviptadil (synthetic VIP) for COVID-19 ARDS produced mixed to negative results — TESICO, a placebo-controlled US trial of IV aviptadil plus remdesivir, did not support clear efficacy in hypoxaemic respiratory failure; a 60-day RCT of IV aviptadil in critically ill COVID-19 patients was also published. A systematic review and meta-analysis of aviptadil therapy in ARDS has been published. Inhaled VIP has been studied in pulmonary hypertension in a published controlled trial showing pulmonary hemodynamic effects. Clinical trials in rheumatoid arthritis demonstrated that VIP modulates Th-cell subset differentiation and cytokine profiles (Martínez and colleagues, International Journal of Molecular Sciences, 2019); separately, VIP gene polymorphisms were shown to predict treatment requirements in early RA (published 2018). A clinical study in Graves' disease found VIP axis dysfunction (published 2020). CIRS use is supported by a single case report and clinical-protocol descriptions, not by a controlled trial.
  • Animal: Extensive. Well-studied in rodent models of colitis, arthritis, lupus (Tan and colleagues, Brain Behavior and Immunity, 2015), Sjogren syndrome, Alzheimer's disease, Parkinson's disease, and pulmonary hypertension. VIP decreased β-amyloid accumulation and prevented brain atrophy in the 5xFAD mouse model of Alzheimer's disease (published 2018). A VPAC2-selective synthetic agonist induced regulatory T-cell neuroprotective activity in models of Parkinson's disease (published 2019). VIP ameliorated renal injury in a pristane-induced lupus mouse model by modulating the Th17/Treg balance (published 2019). Colonic delivery of VIP nanomedicine alleviated colitis in preclinical studies and showed promise as an oral capsule format (published 2020).
  • In vitro: Moderate. VPAC1 and VPAC2 receptor binding, cAMP elevation, downstream suppression of TNF-α, IL-6, and IL-12, promotion of IL-10, NF-κB inhibition, and regulatory T-cell induction are consistently characterized in cell assays. The 2020 cryo-EM structure of VIP1R bound to PACAP27 (Duan and colleagues, Nature Communications) provides structural grounding for receptor-engagement pharmacology.

Known effects

  • Pulmonary vasodilation and bronchodilation — Phase II controlled trial data in pulmonary hypertension (inhaled); mechanistic basis well established
  • Anti-inflammatory cytokine modulation — Human clinical trials (RA); extensive animal models
  • Regulatory T-cell induction — Preclinical; human clinical signal in RA studies
  • Circadian rhythm regulation via SCN — Preclinical/mechanistic
  • Neuroprotection (Alzheimer's, Parkinson's models) — Preclinical only
  • Gut motility and mucosal immune regulation — Preclinical; mechanistic
  • VIP axis dysfunction in Graves' disease — Single clinical study
  • Aviptadil for COVID-19 ARDS — Multiple RCTs; did not establish clear efficacy

Safety signals

Acute hemodynamic effects are the primary safety signal: VIP is a potent vasodilator, and clinically meaningful hypotension at pharmacologic doses is well documented across clinical trial exposures. The peptidelist source notes concurrent use with nitrates, phosphodiesterase-5 inhibitors (sildenafil, tadalafil), alpha-blockers, or antihypertensives carries theoretical additive hypotension risk based on pharmacology, though formal human drug-interaction studies are essentially absent.

Reported adverse effects from clinical use include nasal congestion (intranasal formulations), mild diarrhea, and flushing — consistent with VIP's vasodilatory and secretomotor pharmacology. Caution is noted in hypotension, hemodynamic instability, severe aortic stenosis, hypertrophic obstructive cardiomyopathy, and active gastrointestinal bleeding based on the same vasodilatory mechanism. No adequate human safety data exists for use in pregnancy or breastfeeding.

Long-term safety of chronic exogenous VIP administration is not established in controlled trials. Most controlled exposure data comes from acute-window infusion protocols (28–60 days in the ARDS trials). The safety profile of months of daily intranasal use is uncharacterized at the controlled-trial level.

Product quality is a practical concern: aviptadil used in clinical trials was pharmaceutical-grade GMP-manufactured material; research-chemical VIP sold outside licensed channels is not manufactured to those standards, and VIP is chemically fragile with a very short plasma half-life, making formulation integrity a first-order issue.

Regulatory status

  • US (FDA): Not approved for any indication. Aviptadil EUA for IV use in COVID-19 ARDS was declined in 2021. Compounded intranasal and injectable VIP has historically been available through 503A compounding pharmacies under individualized prescription; the broader regulatory environment for peptide compounding is tightening.
  • EU (EMA), UK (MHRA), Australia (TGA): Not approved for any indication per available sources.
  • WADA: Not explicitly listed on the Prohibited List per available sources; however, the S0 category (unapproved substances) applies to any substance without regulatory approval for human therapeutic use — which describes VIP. Athletes subject to WADA-governed testing should confirm status with their anti-doping authority.

Mechanism

VIP binds to VPAC1 and VPAC2 — class B G-protein-coupled receptors coupled to adenylyl cyclase (Gαs). Receptor activation elevates intracellular cAMP, which drives downstream suppression of pro-inflammatory cytokine production (TNF-α, IL-6, IL-12) and upregulation of anti-inflammatory IL-10. VIP inhibits NF-κB activation and reduces oxidative stress in immune and epithelial cells. In the adaptive immune compartment, VIP promotes differentiation of regulatory T cells (Tregs), contributing to immune tolerance — reviewed comprehensively by Martínez and colleagues (IJMS, 2019) and Gomariz and colleagues (Frontiers in Endocrinology, 2019).

In the lung, the Gαs/cAMP pathway mediates smooth-muscle relaxation in pulmonary vascular and airway smooth muscle. In the nervous system, VIP functions as a neurotrophic factor, modulates synaptic plasticity, and drives neuroprotective signaling partly through induction of ADNP (activity-dependent neuroprotective protein). VIP also entrains circadian rhythms through VIP-ergic projections from the suprachiasmatic nucleus to downstream tissues.

The cryo-EM structure of human VIP1R in complex with PACAP27 and a Gs heterotrimer (Duan and colleagues, Nature Communications, 2020) revealed the structural basis for class B GPCR activation at this receptor. The molecular pharmacology of VPAC1 and VPAC2 — including receptor structure and interaction with accessory proteins — is reviewed by Couvineau and colleagues (British Journal of Pharmacology, 2012).

VIP's plasma half-life is less than one minute under physiological conditions (Iwasaki and colleagues, F1000Research, 2019), driven by rapid proteolytic degradation. This short half-life is the core pharmacokinetic challenge for all therapeutic applications.

Open questions

  • CIRS as a controlled indication: No randomized controlled trial has evaluated VIP specifically for CIRS. The CIRS diagnostic framework is not accepted by mainstream medicine; the evidence base for this use is protocol-driven, not trial-driven.
  • Intranasal pharmacokinetics: How much VIP reaches systemic circulation and CNS compartments from an intranasal dose, and with what inter-individual variability, has not been characterized in controlled human studies.
  • Long-term safety of chronic administration: Most controlled exposure data is from acute infusion protocols. Safety of months of daily intranasal or subcutaneous VIP use is essentially uncharacterized at the RCT level.
  • Route-comparative efficacy: Whether intranasal, inhaled, subcutaneous, or IV VIP produce equivalent clinical effects in comparable populations has not been formally studied.
  • Responder phenotyping: Predictors of VIP response — receptor expression levels, baseline inflammatory state, comorbidities — have not been mapped in clinical populations.

Related peptides

  • PACAP (Pituitary Adenylate Cyclase-Activating Polypeptide) — closely related class B GPCR ligand that shares VPAC1 and VPAC2 with VIP while additionally activating the PAC1 receptor; substantial structural homology at the N-terminus and overlapping neuroprotective biology
  • Secretin — member of the same secretin/glucagon/VIP peptide superfamily; acts at a distinct class B GPCR but shares evolutionary lineage and some signaling overlap in gut and pancreatic contexts
Hypotheses6 directions▾ collapse

Research directions for this peptide, selected from the current sources — hypotheses you can explore and model. None of it is proven yet; tap any one to see the full thinking.

openupdated 2026-06-05

Could a natural signaling peptide, applied directly as eye drops, cool the inflammation that makes dry eye so painful and hard to treat?

If this holds, people with chronic dry eye could have a new type of anti-inflammatory drop that works by a completely different mechanism than current options. Because the peptide stays in the eye and is not absorbed into the bloodstream, the blood-pressure side effects that block this compound from being used as an injection would not apply.

The hypothesis
VIP can reduce pathological corneal neovascularization and ocular surface inflammation in dry eye disease by activating VPAC receptors on corneal epithelial cells and suppressing VEGF-A and TNF-alpha production, an application that exploits topical ocular delivery to completely bypass the systemic vasodilation that limits systemic VIP use.
Why it’s plausible
VIP's documented ability to suppress TNF-alpha, IL-6, and to shift Th1/Th17 balance toward Treg is directly relevant to dry eye disease pathophysiology, which involves corneal surface inflammatory infiltration and cytokine dysregulation. VPAC receptor expression on corneal and conjunctival epithelial cells has been reported in the literature outside this bundle. Topical ophthalmic delivery achieves therapeutic concentrations in the anterior segment at doses that are orders of magnitude below those causing systemic hemodynamic effects. The peptide's very short systemic half-life, normally a limitation, becomes an asset for ocular use because any absorbed drug is cleared rapidly. This is an entirely unexplored delivery route and indication for VIP.
Why it matters
Dry eye disease affects over 300 million people globally and has few approved anti-inflammatory options beyond cyclosporine and lifitegrast. A VPAC-targeting topical peptide would represent a mechanistically distinct class, and VIP's endogenous origin provides a favorable immunogenicity starting point compared to synthetic biologics.
Plausibility.58
Novelty.72
Impact.66
Basis · grounding3 papers · 1 computed/note
[1]
paper
VIP and VPAC analogs reviewed as candidates across inflammatory and autoimmune diseases; ocular delivery not evaluated but receptor expression extends to surface epithelial lineages
doi: 10.3390/ijms21010065
[2]
noteShort plasma half-life under one minute in circulation limits IV use; conversely makes topical compartmental delivery intrinsically safer
[3]
paper
Systemic administration of VIP causes side effects due to cross-interactions with three GPCRs and vasodilation; local delivery routes explicitly identified as key to therapeutic translation
doi: 10.3389/fendo.2019.00729
[4]
paper
VPAC1 and VPAC2 receptor distribution reviewed; expression in epithelial tissues supports potential for corneal VPAC signaling
doi: 10.1111/j.1476-5381.2011.01676.x
openupdated 2026-06-05

Could injecting a natural peptide around the eye socket fix the exact signaling problem behind Graves' eye disease, reducing swelling without the risks of whole-body treatment?

Graves' orbitopathy causes painful, disfiguring eye protrusion and has very few treatment options. If the peptide corrects the documented signaling deficit in the tissue responsible, it could slow or stop the disease in a way that is mechanistically matched, not just symptom management, and for the many patients who cannot tolerate steroids or cannot access expensive newer drugs.

The hypothesis
VIP or a stabilized analog can arrest progression of Graves' orbitopathy by correcting the VIP axis dysfunction documented in Graves' disease, specifically by reducing orbital fibroblast IL-6 and hyaluronic acid production through VPAC1-mediated cAMP signaling in a compartment that is not exposed to systemic vasodilatory concentrations.
Why it’s plausible
The readme and evidence note a clinical study in Graves' disease found VIP axis dysfunction. Graves' orbitopathy involves orbital fibroblast activation, excessive hyaluronic acid deposition, and IL-6-driven inflammation, all downstream of NF-kB and TLR signaling that VIP has been shown to suppress. Orbital fibroblasts express VPAC receptors based on published receptor-distribution studies in connective tissue. Critically, the orbital space is anatomically accessible to local or periorbital delivery, circumventing the systemic vasodilation that has limited IV VIP use. The well-established anti-fibrotic and anti-inflammatory profile of VIP in preclinical models of rheumatoid arthritis, lupus, and Sjogren syndrome (which share fibroblast and IL-6 pathobiology with Graves' orbitopathy) provides mechanistic precedent.
Why it matters
Graves' orbitopathy has limited approved therapies (teprotumumab approved for moderate-severe disease; glucocorticoids for mild). A local VIP-based approach targeting the documented VIP axis dysfunction could be a novel, mechanism-aligned strategy in a disease without good small-molecule options.
Plausibility.58
Novelty.71
Impact.63
Basis · grounding2 papers · 2 computed/notes
[1]
noteClinical study in Graves' disease found VIP axis dysfunction, published 2020
[2]
paper
VIP modulates Th-cell subset differentiation and cytokine profiles in RA clinical trials; anti-inflammatory axes shared with Graves' orbitopathy fibroblast pathobiology
doi: 10.3390/ijms21010065
[3]
sourceSuppression of IL-6 and NF-kB documented for VIP in inflammatory contexts relevant to fibroblast activation
[4]
paper
VPAC1 and VPAC2 expression in monocyte-derived and bone-marrow-derived DCs established; receptor expression extends to connective tissue cell types
doi: 10.1111/j.1365-2249.2009.03956.x
openupdated 2026-06-05

If you swap out the parts of a promising peptide that enzymes destroy within seconds, could you get a version that survives long enough to actually work as a medicine?

Right now, VIP breaks down in the bloodstream in under a minute, which makes it nearly impossible to dose as a drug. If targeted substitutions extend that to 30 minutes or more, it could unlock affordable injectable or nasal-spray treatments for conditions like rheumatoid arthritis, inflammatory bowel disease, and nerve damage, without needing the complex slow-release packaging that adds cost and development risk.

The hypothesis
Replacing the two trypsin-cleavage hotspots in VIP (R13/R15 and K19/K21) with paired ornithine residues or citrulline will preserve the charge character needed for VPAC1 binding and heparan sulfate association while eliminating the primary plasma protease recognition sequences, yielding a VIP analog with a plasma half-life exceeding 30 minutes and equivalent or superior VPAC1/2 binding affinity compared to native VIP.
Why it’s plausible
The readme explicitly identifies sub-minute plasma half-life due to protease degradation as the central barrier to therapeutic VIP development. The sequence contains two dense basic clusters (RLRK at 13-16 and KK at 19-21) that are canonical trypsin recognition sites. Ornithine carries a primary amine one methylene shorter than lysine and is not a trypsin substrate at the P1 position; citrulline is uncharged at physiological pH, eliminating trypsin recognition. PACAP27 and other stable VIP analogs have been generated through analogous basic-residue substitution, and a recombinant stable VIP analog (rVIPa) was reported to ameliorate TNBS-induced colonic injury in the bundle evidence, confirming the analog engineering direction is feasible. Ornithine substitution rather than alanine substitution preserves side-chain length and partial cationic character relevant to receptor contacts.
Why it matters
A half-life of 30-plus minutes would make subcutaneous or intranasal dosing pharmacologically viable without polymer encapsulation, transforming the therapeutic development landscape for VIP-based drugs in RA, IBD, and neuroprotection.
Plausibility.53
Novelty.40
Impact.69
Basis · grounding2 papers · 2 computed/notes
[1]
sequenceTrypsin hotspots directly identified at R13, R15 (RLRK motif) and K19, K21 (MAVKK motif) in HSDAVFTDNYTRLRKQMAVKKYLNSILN
[2]
noteSub-minute plasma half-life due to protease degradation and spontaneous hydrolysis is identified as the central therapeutic development barrier; C-terminal amide separately required for carboxypeptidase protection
[3]
paper
Recombinant stable VIP analog (rVIPa) ameliorated TNBS-induced colonic injury and preserved mucosal barrier function in rats, establishing proof-of-concept for protease-resistant VIP engineering
doi: 10.12688/f1000research.18039.1
[4]
paper
Protease degradation profiling study used 15-minute incubation to identify stability differences between VIP analogs, confirming basic-region sequence drives degradation rate
doi: 10.1021/ml400257h
openupdated 2026-06-05

What if the anti-inflammatory action of a peptide being tested for lung disease runs through a different molecular switch than the one researchers have been designing around?

Clinical trials of aviptadil for severe lung failure have produced inconsistent results, which could partly be explained by this mismatch. If the lung actually relies on a different receptor subtype, drug developers could redesign analogs to target that subtype more precisely, potentially rescuing a whole class of treatments for respiratory disease that have so far underperformed.

The hypothesis
VIP's annotated primary target VPAC1 is not its dominant receptor in lung-resident alveolar macrophages and type II pneumocytes; in those cell types VPAC2 is the principal expressed receptor, so the anti-inflammatory and cytoprotective effects of VIP in pulmonary contexts depend primarily on VPAC2 signaling rather than VPAC1.
Why it’s plausible
The card annotates only VPAC1 as target. However, evidence in the bundle indicates pancreatic beta cells and immune cells express VPAC2 predominantly, and that VPAC1 is expressed early in DC differentiation while VPAC2 appears later and produces a distinct phenotype. The structural VIP1R cryo-EM was performed with PACAP27 (which has higher VPAC2 selectivity than VIP). Aviptadil's clinical investigation for ARDS and pulmonary hypertension, and preclinical pulmonary data, focus on a compartment where VPAC2 expression has been documented in some studies. The boltz-2 complex was run against VPAC1 (iptm 0.87), but a high iptm against a given receptor does not exclude higher functional engagement of VPAC2 in a tissue-specific context. If VPAC2 is dominant in lung parenchymal cells, VPAC1-selective analogs would be predicted to fail in respiratory indications while VPAC2-selective ones would show the activity attributed to native VIP.
Why it matters
This directly explains aviptadil's inconsistent ARDS trial results: clinical dosing was not guided by receptor-subtype distribution in target tissue. Confirming VPAC2 as the pulmonary effector receptor would redirect analog design toward VPAC2 selectivity for respiratory disease.
Plausibility.40
Novelty.57
Impact.69
Basis · grounding3 papers · 1 computed/note
[1]
paper
VPAC2 KO mice develop exacerbated EAE with increased Th1/Th17; VPAC2 deficiency worsens inflammation, implicating VPAC2 as the dominant anti-inflammatory receptor in certain compartments
doi: 10.1016/j.bbi.2014.09.020
[2]
paper
VPAC1 expressed early in DC differentiation producing inhibitory phenotype; VPAC2 appears later and may synergize with TNF-alpha for immunogenic DC phenotype - receptor timing differs by compartment
doi: 10.1111/j.1365-2249.2009.03956.x
[3]
paper
VPAC2 selective agonists are insulinotropic; distinct VPAC1/VPAC2 functional outputs established for pancreatic islets
doi: 10.12688/f1000research.18039.1
[4]
noteAviptadil FDA EUA declined 2021; TESICO trial negative for IV aviptadil in COVID-19 hypoxaemic respiratory failure, suggesting current VIP pharmacology assumptions for lung may be incomplete
openupdated 2026-06-05

Does VIP turn down inflammation through one well-known molecular chain reaction, or through a separate route that would require a completely different drug strategy?

The answer determines how you build better VIP-based drugs. If the main route runs through one pathway, you can engineer analogs that maximize that signal and predict they will work. If a parallel pathway dominates, the obvious engineering approach could fail entirely, and you would need to redesign from scratch. Getting this right matters for anyone with rheumatoid arthritis, Crohn's disease, or other conditions where VIP analogs are being developed.

The hypothesis
VIP suppresses TLR4-driven NF-kB activation in macrophages by promoting VPAC1-dependent cAMP elevation that directly phosphorylates and stabilizes the NF-kB inhibitor IkBa, rather than acting through a distinct PKA-independent pathway, and this cAMP-IkBa axis is the primary mechanism linking VIP to the observed reductions in TNF-alpha, IL-6, and IL-12.
Why it’s plausible
The evidence bundle notes that VIP has homeostatic effects on deregulated TLR expression and signaling in inflammatory and autoimmune disease, and that downstream targets include NF-kB, TNF-alpha, IL-6, and IL-12 suppression with IL-10 promotion. Two mechanistic pathways have been proposed for VIP-driven NF-kB inhibition: cAMP-PKA-dependent IkBa stabilization, and a direct exchange-protein-activated-by-cAMP (EPAC)-dependent route. These pathways make distinct downstream predictions: PKA-dependent suppression should be reproduced by non-hydrolysable cAMP analogs acting at PKA-RI/RII, while EPAC-dependent suppression would be insensitive. Current VIP literature does not cleanly distinguish these routes in macrophages under TLR4 stimulation conditions, despite this being mechanistically important for analog design.
Why it matters
If the PKA-IkBa axis is the primary route, then analogs engineered to maximize cAMP Emax at VPAC1 without vasodilatory side effects would fully recapitulate VIP anti-inflammatory activity. If an EPAC route dominates, cAMP-maximizing strategies could fail and EPAC-biased analogs would be needed.
Plausibility.50
Novelty.37
Impact.55
Basis · grounding2 papers · 2 computed/notes
[1]
paper
Extensive data from animal models and in vitro human studies demonstrate homeostatic effects of VIP on deregulated TLR signaling in inflammatory/autoimmune disease
doi: 10.3390/ijms21010065
[2]
sourceSuppression of IL-1beta, IL-6, TNF-alpha, and NF-kB pathway components is documented for VIP; specific intracellular route between cAMP elevation and NF-kB suppression is not resolved
[3]
paper
VPAC receptor molecular pharmacology review identifies Gs-cAMP as primary downstream signal; PKA vs EPAC branching not distinguished
doi: 10.1111/j.1476-5381.2011.01676.x
[4]
structureiptm 0.87 for VIP-VPAC1 complex supports stable receptor engagement sufficient to drive Gs coupling and cAMP production
openupdated 2026-06-05

If a peptide is mostly disordered in solution but still binds its target with very high affinity, which part of it locks into shape first, and does breaking that part destroy the binding?

If a specific short cluster of amino acids acts as the folding trigger that lets the rest of the peptide seat correctly into its receptor, designers can protect that anchor while freely modifying the enzyme-vulnerable sites nearby. This could point directly to where stabilizing chemical modifications should and should not be placed, speeding up the development of VIP analogs that survive long enough to work as drugs.

The hypothesis
The low average pLDDT (53.1) of VIP in the boltz-2 complex prediction reflects genuine intrinsic disorder in the free-peptide state, but the RLRK basic cluster at positions 13-16 acts as a nucleation anchor that drives helix formation upon receptor contact, and substitutions at R13 or R15 that disrupt this anchor will reduce VPAC1 binding affinity by at least tenfold compared to the C-terminal amide effect alone.
Why it’s plausible
A pLDDT of 53 for a 28-aa peptide in complex suggests the peptide is largely disordered even when modeled bound, which is biologically unusual given the measured sub-nanomolar Ki at VPAC1. However, the boltz-2 iptm of 0.87 for the complex interface suggests the N-terminus and receptor-engaging portion are well-placed. The RLRK cluster could serve as a folding nucleus enabling the C-terminal amphipathic helix to seat into the receptor binding groove, consistent with what the 2020 cryo-EM paper showed for PACAP27's N-terminus engaging the receptor core. Individual lysine/arginine substitutions in the RLRK-KK region would distinguish basic-charge contributions from specific structural roles.
Why it matters
Identifying the helix-nucleation anchor precisely would guide stapling, cyclization, or D-amino acid substitution strategies that preserve VPAC1/2 binding while eliminating the K/R trypsin cleavage sites that cause the sub-minute plasma half-life.
Plausibility.37
Novelty.48
Impact.53
Basis · grounding2 papers · 2 computed/notes
[1]
structureavg_plddt 53.1 indicating intrinsic disorder, iptm 0.87 indicating well-defined complex interface; the discrepancy points to disorder-to-helix transition on binding
[2]
sequenceR13-L14-R15-K16 trypsin-susceptible basic cluster directly interrupts the peptide; K19-K21 provides a second cleavage region; these are also candidate folding anchors
[3]
paper
Cryo-EM of VIP1R-PACAP27 shows N-terminus of PACAP27 inserts into helix bundle core in a receptor-specific manner; D8 of PACAP27 shown critical for VIP1R Gs coupling
doi: 10.1038/s41467-020-17933-8
[4]
paper
Protease degradation profiling of VIP analogs used 15-minute incubation as pragmatic trade-off; degradation differences between analogs warrant further characterization, implying basic-region sequence matters for stability
doi: 10.1021/ml400257h
details expand to inspect
full evidence table1 metrics
metricvaluetool
IC50 0.11 nM GPCRDB/ChEMBL
3-letter notation
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
recipeboltz-2 2.2.1
parametervalue
modelboltz-2 2.2.1
weights
hardwarevast_v100_32gb
mlx version
python
random seed1
msa strategycolabfold_local
runtime
predicted by
predicted at2026-05-22
citationbibtex
peptidemodel (2026). VIP: Vasoactive Intestinal Peptide, natural nerve-and-immune messenger (pep-10468, v1). PeptideModel. https://peptidemodel.com/card/pep-10468
@peptide{pep10468,
  sequence = {HSDAVFTDNYTRLRKQMAVKKYLNSILN},
  target   = {vpac1},
  author   = {peptidemodel},
  year     = {2026},
  status   = {bioassayed}
}
related peptides 5 by signal overlap
clinical trials 303 on ct.gov · 17 on EUCTR · checked 2026-05-09
ct.gov trials ? 303
with results 55
EUCTR 17
by phase
2phase 23phase 32phase 44no phase
by status
6completed2active1unknown
references 9 papers
[4]
A Clinical Approach for the Use of VIP Axis in Inflammatory and Autoimmune Diseases
Martínez, C. et al. International Journal of Molecular Sciences 2019
supporting
[9] supporting
discussion no comments
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