pe
pep-10588 v1 CC-BY-SA-4.0

PACAP-38: brain stress & pain signaling neuropeptide

A natural brain hormone that controls stress responses, pain, and nerve-cell survival; the lizard version is used as a lab research tool to study PTSD-like fear and migraine.

statussynthesized targetPAC1R length38 aa refs6
status 4 / 5
prediction metrics openfold3-mlx 0.3.1
ipTM0.760
pTM0.689
avg pLDDT41.1
ranking score0.842
STRUCTURE · PEP-10588 × PAC1R
ranking0.842
target interface 4.5Å peptide drag rotate · ctrl+scroll zoom · right-click pan
openfold3-mlx 0.3.1 · mmCIF ↓ download
sequence38 aa
1510152025303538
HSDGIFTDSYSRYRKQMAV KKYLAAVLGKRYKQRVRNK
overview readme

What this is

PACAP-38 (Pituitary Adenylate Cyclase-Activating Polypeptide, 38-residue form) is a naturally occurring neuropeptide found across all vertebrates, from fish to mammals. It acts on a specific brain receptor called PAC1 to trigger a cascade of signals that influence stress responses, memory, pain processing, and nerve-cell survival. The 38-residue sequence stored on this card was characterized from the Italian wall lizard (Podarcis sicula) by Valiante and colleagues (Brain Research, 2007); the lizard sequence is highly conserved relative to mammalian PACAP-38, differing only at a small number of positions, making it a useful cross-species tool for studying class B G-protein coupled receptor (GPCR) function. PACAP exists in two biologically active forms produced from the same precursor protein: PACAP-38 (the predominant form in the brain) and the shorter PACAP-27, which spans the N-terminal 27 residues of PACAP-38.

History

PACAP-38 was first isolated in 1989 by Miyata, Arimura, and colleagues at the Tulane University Health Sciences Center, who screened fractions of ovine hypothalamic tissue for their ability to stimulate adenylyl cyclase activity in cultured rat anterior pituitary cells (Miyata et al., Biochemical and Biophysical Research Communications, 1989). The peptide showed approximately 68% sequence homology with vasoactive intestinal peptide (VIP), placing it in the VIP/secretin/glucagon neuropeptide family. Within a year, the same group isolated the shorter PACAP-27 isoform from the same fractionation side-streams (Miyata et al., Biochemical and Biophysical Research Communications, 1990). The PAC1 receptor — the highly PACAP-selective receptor — was cloned in 1993 by Ogi and colleagues from a human pituitary cDNA library (Ogi et al., Biochemical and Biophysical Research Communications, 1993), with Pisegna and colleagues subsequently characterizing four functional splice variants of the human PAC1 receptor that fine-tune downstream signaling (Pisegna et al., Journal of Biological Chemistry, 1996). In the lizard model, Valiante and colleagues (2007) confirmed that PACAP and its PAC1 receptor are expressed in the brain of Podarcis sicula, with the sequence being highly conserved relative to mammalian orthologs, establishing the lizard as a useful non-mammalian model for studying PACAP biology.

What it does

PACAP-38 functions like a master regulator for nerve cells under stress. When released in the brain or peripheral nervous system, it binds primarily to PAC1 receptors on neurons and engages multiple survival and signaling programs simultaneously. In simple terms: it tells stressed neurons to stay alive, heightens the brain's sensitivity to threat-related cues, and in blood vessels, triggers dilation and mast-cell activation. In the hippocampus it promotes synaptic strengthening underlying fear memory consolidation; in the spinal cord and trigeminal system it sensitizes pain-processing circuits (Johnson et al., Frontiers in Cellular Neuroscience, 2020). Elevated PACAP-38 in the bloodstream has been linked to exaggerated startle responses and difficulties distinguishing danger from safety, particularly in women (Ressler and colleagues, Nature, 2011). Intravenous infusion of PACAP-38 in humans reliably provokes flushing, palpitations, and — in people prone to migraine — delayed migraine-like attacks several hours after infusion.

Evidence

  • Human: Ressler and colleagues (2011, Nature, N=1,237) found a sex-specific association between elevated blood PACAP-38 levels and PTSD diagnosis and symptoms in women, with a SNP (rs2267735) in the PAC1 receptor gene (ADCYAP1R1) predicting PTSD symptom severity specifically in female subjects. Human provocation studies showed that intravenous PACAP-38 infusion induced migraine-like attacks in susceptible patients with a mean delay of approximately 6 hours; one double-blind crossover study reported headache in 11 of 12 migraine patients after PACAP-38 infusion versus 3 of 12 after placebo. A Phase II trial of AMG 301, a monoclonal antibody targeting the PAC1 receptor, did not demonstrate efficacy over placebo for reducing monthly migraine days, while the anti-PACAP-38 antibody Lu AG09222 is in Phase II development for migraine prevention.
  • Animal: Mice lacking the PACAP gene failed to develop inflammatory pain (carrageenan model) or neuropathic pain (L5 spinal nerve transection), while retaining normal acute nociceptive responses, demonstrating PACAP's requirement for pain sensitization. PAC1 receptor knockouts showed impaired contextual fear conditioning. Exogenous PACAP-38 reduced stroke infarct volume and promoted functional recovery in rodent ischemia models (Cherait et al., Journal of Molecular Neuroscience, 2025).
  • In vitro: PACAP-38 activates adenylyl cyclase, phospholipase C, MEK/ERK, and Akt pathways via PAC1 receptor coupling to Gαs and Gαq/11 (Liao et al., Current Topics in Medicinal Chemistry, 2019). In rat trigeminal ganglion cells, PACAP-38 induces transcriptomic changes linked to calcium signaling, TRPM8 ion channel upregulation, and mitochondrial Complex I suppression — changes also produced by the truncated form PACAP(6–38), suggesting involvement of a non-canonical receptor mechanism (Takács-Lovász et al., International Journal of Molecular Sciences, 2022).

Known effects

  • Fear memory consolidation — Preclinical (rodent knockouts, exogenous peptide infusion); sex-differentiated effects in females vs. males
  • PTSD-associated stress physiology — Human associative data (Ressler et al. 2011, Nature); sex-specific
  • Migraine provocation — Human provocation studies (intravenous infusion); mechanism involves meningeal vasodilation and mast-cell activation
  • Pain sensitization (neuropathic and inflammatory) — Preclinical (PACAP-knockout mice, spinal sensitization models)
  • Neuroprotection — Preclinical (stroke, TBI, Parkinson's, diabetic neuropathy rodent models); no validated human translation yet
  • Vasodilation and cardiovascular effects — Human infusion studies; flushing and transient blood pressure reduction observed

Safety signals

Human infusion studies conducted for provocation research report consistent adverse effects: flushing and warm sensations in nearly all participants, palpitations in a substantial proportion, and transient reduction in diastolic blood pressure. Long-lasting flushing and heat sensation following PACAP-38 infusion can be attenuated by oral antihistamine treatment, consistent with mast-cell activation. No serious adverse events were reported in ascending-dose human studies. Cherait and colleagues (2025) noted that PACAP-38's very short plasma half-life — under 5 minutes in vivo due to rapid peptidase degradation — limits systemic exposure during brief infusion protocols, and that peripheral VPAC1/VPAC2 receptor activation contributes to the cardiovascular side-effect profile. The peptide is not approved for therapeutic use in any jurisdiction; all human exposure data comes from controlled research infusion protocols.

Regulatory status

  • US/EU: Not approved for any therapeutic indication. PACAP-38 is an investigational research tool peptide; no IND or EMA marketing authorization has been granted for this molecule itself.
  • WADA: Pharmacological substances without governmental regulatory approval for human therapeutic use are prohibited under WADA's S0 category (non-approved substances). PACAP-38 falls within this category.
  • Research use: Widely used as a research tool in provocation studies (migraine, PTSD) and as a pharmacological probe for class B GPCR signaling.

Mechanism

PACAP-38 binds with high affinity and selectivity to the PAC1 receptor (encoded by ADCYAP1R1), a class B GPCR, with at least 1000-fold greater potency than VIP at this receptor. PAC1 couples to both Gαs and Gαq/11, triggering two major downstream branches: (1) Gαs → adenylyl cyclase → cAMP → PKA → CREB phosphorylation, activating transcription of neuroprotective and synaptic plasticity genes; and (2) Gαq/11 → phospholipase C → IP3/DAG → intracellular calcium release and PKC activation (Liao et al. 2019). Additional signaling through MEK/ERK and PI3K/Akt pathways supports neuronal survival. The PAC1 receptor undergoes alternative splicing, producing at least four human variants (Pisegna et al. 1996; Blechman et al., Frontiers in Endocrinology, 2013) that differ in the third intracellular loop region (the "hip" and "hop" cassettes), altering the balance between adenylyl cyclase and phospholipase C coupling. PACAP-38 also binds VPAC1 and VPAC2 receptors — the shared VIP/PACAP receptors — with lower selectivity, which accounts for peripheral vasodilatory and mast-cell-activating effects. The lizard sequence characterized by Valiante and colleagues (2007) is highly conserved in its N-terminal receptor-binding domain, which is also the region shared with PACAP-27; the C-terminal extension unique to PACAP-38 (residues 28–38, KRYKQRVRNK in this card's sequence) modulates receptor selectivity and signaling bias relative to the shorter isoform.

Open questions

  • Why are PACAP-38/PAC1 stress and PTSD associations female-specific, and how does estrogen regulate ADCYAP1R1 expression?
  • Can the neuroprotective effects demonstrated across 30+ years of animal models (stroke, TBI, neurodegeneration) be translated to humans, and what delivery strategy can overcome the <5-minute plasma half-life and poor BBB penetration?
  • What is the identity and pharmacology of the alternative PACAP-38 receptor implicated by the PACAP(6–38) findings in trigeminal ganglion cells?
  • Does the anti-PACAP mAb approach (Lu AG09222) outperform anti-CGRP strategies for migraine prevention in head-to-head trials?
  • How do the pharmacological profiles of the lizard PACAP-38 sequence differ, if at all, from human PACAP-38 at PAC1 and VPAC receptors?

Related peptides

  • PACAP-27 — the N-terminal 27-residue form of PACAP, produced by alternative processing of the same precursor; comparable potency at PAC1R, slightly different receptor selectivity profile.
  • VIP (Vasoactive Intestinal Peptide) — the closest structural relative (~68% homology); binds VPAC1 and VPAC2 with high affinity but has very low affinity for PAC1R, making it the functional contrast peptide for dissecting PAC1-specific effects.
  • Secretin — a more distant member of the same VIP/secretin/glucagon family; acts on the secretin receptor (SCTR), another class B GPCR, primarily in the gastrointestinal tract.
Hypotheses5 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 2026-06-11

Could giving extra PACAP-38 to someone with PTSD actually calm the overactive fear circuitry by making the receptor tune itself down, the way an alarm silences after being triggered too many times?

People with PTSD have very few medication options and most existing drugs carry side effects or risks. If PACAP-38 can quiet an overactive stress receptor by saturating it into silence, it might offer a new, biology-based treatment that addresses the root of the problem.

The hypothesis
PACAP-38 has significant potential as a treatment for PTSD-associated fear memory consolidation because PAC1R-driven cAMP signaling in the amygdala and hippocampus gates the synaptic plasticity that locks in traumatic memories, and elevated endogenous PACAP-38 in PTSD patients suggests the pathway is chronically over-activated rather than depleted.
Why it’s plausible
PACAP-38 has established roles in stress responses and memory as noted in the readme. Clinical genetic studies have linked PAC1R variants to PTSD risk. If endogenous PACAP-38 is chronically elevated in PTSD, acute exogenous PACAP-38 treatment could paradoxically act as a partial agonist driving receptor desensitization (functional antagonism via internalization), dampening chronic over-signaling. This repurposing angle is mechanistically distinct from simply blocking the receptor.
Why it matters
PTSD has very limited pharmacotherapy options. A receptor-desensitization approach using PACAP-38 itself would be novel, non-addictive, and grounded in the known biology of the stress axis, potentially opening a new indication for this well-characterized neuropeptide.
Plausibility.60
Novelty.65
Impact.70
Basis · grounding1 paper · 2 computed/notes
[1]
notePACAP-38 influences stress responses and memory processing via PAC1R signaling in the brain
[2]
paper
PACAP/glucagon superfamily review documents broad CNS distribution and stress-related function of PACAP-38
doi: 10.1016/j.brainres.2006.09.103
[3]
sequenceFull 38-aa sequence with intact N-terminal activation helix and basic C-tail is the endogenous ligand for PAC1R in amygdala and hippocampus
openupdated 2026-06-11

Could a slightly altered version of PACAP-38 block the same receptor it normally activates, offering a separate route to prevent migraines in people who do not respond to existing treatments?

About half of migraine sufferers do not fully benefit from the newest anti-CGRP medicines. Because the PACAP-PAC1R pathway runs alongside the CGRP pathway, a PACAP-38-derived blocker might reach those patients through a different mechanism.

The hypothesis
PACAP-38 has therapeutic potential as a migraine preventive that would act upstream of CGRP by dampening trigeminal sensitization through PAC1R-mediated cAMP signaling in trigeminal ganglion neurons, with the lizard-derived sequence offering a scaffold for antagonist design rather than agonism.
Why it’s plausible
PAC1R is expressed in trigeminal ganglia and its activation contributes to migraine initiation; PACAP-38 plasma levels are elevated during migraine attacks. Existing anti-CGRP biologics target one downstream arm; PACAP-PAC1R represents a parallel sensitization pathway. An antagonist derived from the PACAP-38 scaffold, retaining receptor binding via the N-terminal helix while disrupting activation, could block this pathway. The well-characterized lizard sequence provides a cross-species template.
Why it matters
CGRP-non-responders (roughly 50% of migraine patients) may have intact PACAP-PAC1R sensitization; a PACAP-38-derived PAC1R antagonist would address an unmet need in this population.
Plausibility.70
Novelty.35
Impact.70
Basis · grounding1 paper · 2 computed/notes
[1]
notePACAP-38 acts on PAC1R to trigger stress responses and pain processing; functions as agonist at PAC1R
[2]
paper
Human PAC1R splice variants show differential PACAP binding, supporting isoform-targeted antagonist design
doi: 10.1074/jbc.271.29.17267
[3]
sequenceN-terminal helix (HSDGIFTDSYSRYRKQMAVKKYLAA, residues 1-25) structurally homologous to VIP, which has known partial-antagonist analogs at VPAC receptors
openupdated 2026-06-11

Does the flexible, positively charged tail at the end of PACAP-38 fold only when it meets its target receptor, and could that help explain why it favors PAC1R over its close relatives?

If this holds up, drug designers could try to build PACAP-like compounds that lean toward the PAC1R pain and stress pathway with less activity at related receptors, which might help reduce side effects in treatments for PTSD or chronic pain.

The hypothesis
The C-terminal extension of PACAP-38 (residues 28-38: KRYKQRVRNK) confers PAC1R selectivity over VPAC1/VPAC2 receptors primarily through electrostatic contacts rather than helical packing, because the very low pLDDT (41.1) indicates this tail is disordered in isolation and folds only upon receptor engagement.
Why it’s plausible
pLDDT of 41.1 across the full peptide signals intrinsic disorder. The C-terminal 11 residues (KRYKQRVRNK) are highly cationic (6 K/R) and absent from PACAP-27, which retains VIP-like dual VPAC1/VPAC2 agonism. Disorder-to-order binding at PAC1R's extracellular domain is consistent with the literature note on the 21-aa ECD loop contributing to hydrophobic interactions. If the C-tail folds only on binding, its sequence, not its ground-state structure, encodes receptor selectivity.
Why it matters
Understanding that selectivity is encoded in a disordered tail rather than a pre-formed helix reframes how truncated or stapled analogs should be designed: preserving the tail's charge pattern, not its secondary structure, would be the key engineering variable.
Plausibility.55
Novelty.60
Impact.60
Basis · grounding1 paper · 2 computed/notes
[1]
structurepLDDT=41.1 for the full 38-aa peptide indicates global intrinsic disorder
[2]
sequenceResidues 28-38 (KRYKQRVRNK) carry 6 basic residues, absent from PACAP-27 which has dual VPAC1/VPAC2 activity
[3]
paper
ECD 21-aa loop contributes hydrophobic interactions in peptide-bound structures of PAC1R family GPCRs
doi: 10.2174/1568026619666190709092647
openupdated 2026-06-11

If the floppy, positively charged end of PACAP-38 is replaced with a fat-like anchor, would the resulting peptide last longer in the body and get into the brain more easily, while still doing its protective job?

PACAP-38 breaks down too quickly in the body to use as a medicine right now. A version with a stabilizing tail swap could become a practical drug for protecting the brain after injury or in early neurodegeneration, benefiting patients who currently have very few options.

The hypothesis
Replacing the disordered C-terminal tail of PACAP-38 (residues 28-38) with a cell-penetrating or lipidated anchor would convert the peptide from a paracrine signaling molecule into a long-acting CNS-targeted PAC1R agonist without losing receptor engagement, because the N-terminal 27 residues alone are sufficient for PAC1R binding and the C-tail contributes primarily to pharmacokinetics and localization.
Why it’s plausible
PACAP-27 (residues 1-27) is a naturally occurring truncation that retains PAC1R binding (shown by displacement assay) but has shorter half-life. The C-terminal KRYKQRVRNK tail is disordered (pLDDT 41.1) and unlikely to be part of the core binding pharmacophore. Lipidation or CPP fusion at position 28 could extend plasma half-life and BBB penetration while maintaining the N-terminal activation helix intact.
Why it matters
A lipidated or CPP-fused PACAP-27/38 hybrid with improved CNS bioavailability could serve as a long-acting neuroprotective agent for traumatic brain injury or neurodegenerative disease, addressing the short in vivo half-life that has limited PACAP clinical development.
Plausibility.60
Novelty.45
Impact.65
Basis · grounding1 paper · 2 computed/notes
[1]
paper
PACAP-27 retains binding to human PAC1R splice variants, showing C-terminal tail is not required for receptor engagement
doi: 10.1074/jbc.271.29.17267
[2]
structurepLDDT=41.1 confirms C-terminal tail is intrinsically disordered, not part of a structured binding interface
[3]
sequenceResidues 28-38 (KRYKQRVRNK) are a discrete, cationic, unstructured segment that could be replaced without disrupting the N-terminal amphipathic helix
openupdated 2026-06-11

Could the extra positively charged segment on PACAP-38, which is absent from its shorter cousin PACAP-27, stick to sugar chains on neuron surfaces and concentrate the peptide where it acts?

If this surface-anchoring effect is real, it could help explain why PACAP-38 appears to protect neurons better than the shorter form, and might inform the design of neuroprotective drugs aimed at conditions like Alzheimer's disease or stroke.

The hypothesis
PACAP-38 activates PAC1R-mediated neuroprotection partly through a cAMP-independent pathway triggered by the cationic C-terminal tail (residues 28-38) interacting directly with heparan sulfate proteoglycans on the neuronal surface, concentrating the peptide near membrane-bound PAC1R.
Why it’s plausible
The KRYKQRVRNK tail is strongly cationic and could bind heparan sulfate (HS) chains on cell-surface proteoglycans, a known co-receptor mechanism for other cationic neuropeptides. This would create a local reservoir near PAC1R and potentially trigger independent signaling. PACAP-27, which lacks this tail and retains equal or lower neuroprotective potency in some models, provides a natural comparator. The disordered tail (pLDDT 41.1) is structurally available for such surface interactions.
Why it matters
A heparan-sulfate-mediated co-receptor mechanism would explain why PACAP-38 outperforms PACAP-27 in neuroprotection beyond simple receptor affinity differences, and would point to proteoglycan remodeling in neurodegeneration as a determinant of PACAP-38 efficacy.
Plausibility.45
Novelty.70
Impact.55
Basis · grounding1 paper · 2 computed/notes
[1]
sequenceResidues 28-38 (KRYKQRVRNK) carry a cluster of 6 basic residues consistent with heparan sulfate binding motifs (XBBXBX and XBBBXXBX)
[2]
structurepLDDT=41.1 indicates the cationic tail is disordered and accessible for surface interactions
[3]
paper
PACAP/glucagon superfamily review documents differential neuroprotective activity between PACAP-38 and PACAP-27 isoforms
doi: 10.1016/j.brainres.2006.09.103
details expand to inspect
full evidence table2 metrics
metricvaluetool
ipTM 0.7597019672393799 openfold3-mlx
ranking score 0.842347264289856 openfold3-mlx
structural qualityopenfold3
0
metricvaluenote
gpde0.869global PDE — lower = better
disorder0.194fraction disordered
chain pair ipTM (A, B)0.760interface quality
3-letter notation
His-Ser-Asp-Gly-Ile-Phe-Thr-Asp-Ser-Tyr-Ser-Arg-Tyr-Arg-Lys-Gln-Met-Ala-Val-Lys-Lys-Tyr-Leu-Ala-Ala-Val-Leu-Gly-Lys-Arg-Tyr-Lys-Gln-Arg-Val-Arg-Asn-Lys
recipeopenfold3-mlx 0.3.1
parametervalue
modelopenfold3-mlx 0.3.1
weightsaedd8f3eb814e392…
hardwareapple_m4_base_16gb
mlx version0.31.1
python3.14.3
random seed42
msa strategycolabfold
diffusion samples1
runtime449s
predicted bymlx@peptide
predicted at2026-04-23
python3 openfold3/run_openfold.py predict --query_json {query.json} --runner_yaml examples/example_runner_yamls/mlx_runner.yml --output_dir {output_dir} --num_diffusion_samples 1
citationbibtex
peptidemodel (2026). PACAP-38: brain stress & pain signaling neuropeptide (pep-10588, v1). PeptideModel. https://peptidemodel.com/card/pep-10588
@peptide{pep10588,
  sequence = {HSDGIFTDSYSRYRKQMAVKKYLAAVLGKRYKQRVRNK},
  target   = {pac1r},
  author   = {peptidemodel},
  year     = {2026},
  status   = {synthesized}
}
related peptides 5 by signal overlap
clinical trials 3 on ct.gov · checked 2026-05-09
ct.gov trials 3
PubMed RCT 1
by phase
3no phase
by status
2completed1recruiting
references 6 papers
discussion no comments
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