pe
pep-10581 v1 CC-BY-SA-4.0

PACAP-38: brain signaling peptide linked to stress, pain, and migraine

A natural nervous-system peptide that regulates stress responses, fear, and pain signaling in the brain; studied for its role in PTSD and migraine, used as a lab research tool.

statussynthesized targetPAC1R length38 aa refs8
status 4 / 5
prediction metrics openfold3-mlx 0.3.1
ipTM0.762
pTM0.698
avg pLDDT41.5
ranking score0.844
STRUCTURE · PEP-10581 × PAC1R
ranking0.844
target interface 4.5Å peptide drag rotate · ctrl+scroll zoom · right-click pan
openfold3-mlx 0.3.1 · mmCIF ↓ download
sequence38 aa
1510152025303538
HIDGIFTDSYSRYRKQMAV KKYLAAVLGKRYKQRVKNK
overview readme

What this is

Pituitary adenylate cyclase-activating polypeptide-38 (PACAP-38) is a 38-amino-acid signaling peptide found in the nervous system of virtually all vertebrates. It belongs to the secretin/glucagon/VIP peptide family and was first isolated in 1989 by Miyata and colleagues from ovine hypothalamic extracts, identified by its ability to stimulate cyclic AMP production in pituitary cells. PACAP-38 is the dominant naturally occurring form of the peptide; a shorter 27-amino-acid variant, PACAP-27, arises from the same precursor through internal cleavage. The sequence stored here was characterized from a chicken gene that encodes both PACAP and growth hormone-releasing hormone (GHRH) on the same locus — a single-gene arrangement unique to birds that was resolved in mammals through gene duplication (McRory et al., DNA and Cell Biology, 1997). Native PACAP-38 carries a C-terminal amide group not represented in the raw stored sequence; research has shown this modification is not required for PAC1 receptor activation (Bourgault et al., 2016).

History

PACAP was discovered in 1989 when Miyata and Arimura screened ovine hypothalamic fractions for their capacity to stimulate cAMP in anterior pituitary cells, identifying a factor roughly 1,000-fold more potent than the related peptide VIP. Two years of structural work yielded both the 38-residue and 27-residue forms. The peptide's remarkable evolutionary stability — differing by only one residue between chicken and most mammals — pointed to fundamental biological importance, and by the early 1990s its receptors had been cloned and characterized in humans and rats (Ogi et al., Biochemical and Biophysical Research Communications, 1993; Hosoya et al., Biochemical and Biophysical Research Communications, 1993). The avian gene encoding PACAP was characterized by McRory and colleagues in 1997, revealing that in chickens the PACAP and GHRH sequences reside on a single co-expressed gene — a feature that in mammals became two separate genes after a stem-mammalian duplication. The 2000s brought detailed work on PAC1 receptor splice variants and intracellular signaling diversity (Pisegna et al., Journal of Biological Chemistry, 1996), and by the 2010s PACAP had been identified as a central player in stress circuitry, fear memory, and migraine — making it one of the most pleiotropic neuropeptides known.

What it does

PACAP-38 acts on neurons and glial cells throughout the brain to adjust the intensity of cellular responses to stress and sensory input. In the hippocampus it enhances the excitability of dentate gyrus granule cells and supports the type of synaptic strengthening that underlies learning and memory (Johnson et al., Frontiers in Cellular Neuroscience, 2020). In stress and fear circuits — particularly the amygdala and bed nucleus of the stria terminalis — elevated PACAP activity amplifies the startle response and can impair the brain's ability to distinguish genuine danger signals from safe ones. In the trigeminovascular system, PACAP-38 dilates meningeal blood vessels and sensitizes second-order pain-processing neurons in a manner that closely replicates the delayed headache and central sensitization seen in migraine attacks (Rubio-Beltrán et al., Journal of Headache and Pain, 2018). Beyond the nervous system, PACAP-38 regulates hormone secretion from the pituitary and pancreas, modulates immune responses, and has been proposed as a neuroprotective factor after ischemic injury (Hashimoto, Yakugaku Zasshi, 2002).

Evidence

  • Human: Intravenous infusion of PACAP-38 in healthy volunteers and migraine patients provoked headache in the large majority of participants, with migraine-like attacks developing with a delayed onset of several hours in susceptible individuals (Rubio-Beltrán et al., 2018). Elevated PACAP-38 blood levels predict PTSD symptom severity in women; a specific single-nucleotide polymorphism in the PAC1 receptor gene (ADCYAP1R1 rs2267735) associates with PTSD and with impaired fear discrimination, with the effect driven by females (Ressler et al., 2011). A Phase 2 trial of AMG 301, a monoclonal antibody targeting the PAC1 receptor, did not separate from placebo for migraine prevention in 343 patients (Ashina et al., Cephalalgia, 2021). A subsequent Phase 2 trial of LY3451838, an antibody neutralizing PACAP-38 itself, showed numerical reductions in monthly migraine days in treatment-resistant patients but likewise did not reach statistical significance (Johnson et al., Cephalalgia, 2025).
  • Animal: PAC1 receptor knockout mice show impaired long-term potentiation in the dentate gyrus and deficits in contextual fear conditioning (Johnson et al., 2020). Fear conditioning increases PAC1 receptor mRNA in the mouse amygdala; estrogen replacement selectively elevates PACAP transcripts in the bed nucleus of the stria terminalis, linking sex-specific stress vulnerability to PACAP tone (Ressler et al., 2011). Preclinical studies with the PAC1 antibody AMG 301 reduced evoked nociceptive activity in the trigemino-cervical complex comparably to sumatriptan (Rubio-Beltrán et al., 2018).
  • In vitro: PACAP-38 activates multiple intracellular pathways downstream of PAC1, including adenylyl cyclase/cAMP, phospholipase C, and MEK/ERK; in dentate gyrus granule cells, PAC1 receptor endosomal recruitment of the MEK/ERK pathway — not the cAMP cascade — is the primary driver of excitability changes (Johnson et al., 2020). The receptor's signaling profile is further shaped by which of several splice variants is expressed, including forms with or without "Hip" and "Hop" inserts in the third intracellular loop (Pisegna et al., 1996).

Known effects

  • Fear sensitization and PTSD vulnerability — Human genetic and biomarker evidence (Ressler et al., 2011); preclinical circuit mapping in amygdala and BNST
  • Migraine provocation — Human infusion studies showing delayed headache and central sensitization; mechanistic evidence via trigeminovascular PAC1 activation
  • Hippocampal neuroplasticity and memory consolidation — Preclinical (LTP and fear conditioning data in knockout and pharmacological models)
  • Stress hormone regulation — Preclinical; PACAP drives CRH and ACTH release in hypothalamic–pituitary–adrenal axis models
  • Growth hormone secretion (avian) — Demonstrated in grass carp and chicken pituitary cells via cAMP and Ca²⁺ signaling (Wong et al., Endocrinology, 2005; McRory et al., 1997)

Safety signals

PACAP-38 is an endogenous neuropeptide with no approved therapeutic application; safety data come from controlled infusion studies and early-phase antibody trials. Human PACAP-38 infusions reproducibly induce headache and, in migraine-susceptible individuals, migraine-like attacks with autonomic features; premonitory symptoms were reported in 48% of migraine patients versus 9% with CGRP infusions (Rubio-Beltrán et al., 2018), suggesting a stronger central component than CGRP-mediated migraine. No serious adverse events were attributed to PACAP-38 itself in published provocation studies. In the Phase 2 AMG 301 antibody trial, adverse-event rates were similar between active and placebo groups (Ashina et al., 2021). The Phase 2 LY3451838 trial reported one serious adverse event (primary CNS lymphoma) assessed as unrelated to the investigational antibody (Johnson et al., 2025).

Regulatory status

  • US: Not approved for any therapeutic indication. Used as a research peptide and in controlled human provocation studies. No FDA IND status publicly registered for PACAP-38 as a therapeutic agent.
  • WADA: No specific listing identified for PACAP-38 on the WADA Prohibited List; as an endogenous peptide with no established performance-enhancing use, it does not currently appear on published prohibited substance schedules.

Mechanism

PACAP-38 signals through three class B GPCRs: PAC1 (encoded by ADCYAP1R1), VPAC1, and VPAC2. PAC1 is roughly 100-fold more selective for PACAP over the structurally related VIP, accounting for PACAP's distinct biological profile relative to VIP at the same tissues (Liao et al., Current Topics in Medicinal Chemistry, 2019). Canonical PAC1 activation stimulates adenylyl cyclase (raising intracellular cAMP) and phospholipase C; the receptor also recruits MEK/ERK signaling after clathrin-mediated endosomal internalization, and in hippocampal dentate gyrus granule cells this endosomal ERK pathway — not the cAMP arm — is the dominant driver of neuronal excitability (Johnson et al., 2020). PAC1 exists in multiple splice isoforms defined by the presence or absence of Hip and Hop cassette inserts in the third intracellular loop; in the mammalian CNS, PAC1-Null and PAC1-Hop predominate, and the ratio of these variants influences downstream signaling bias. In stress circuits, PACAP-expressing terminals in the amygdala and BNST synapse onto PAC1-expressing neurons; elevated PACAP tone in these circuits increases threat-reactivity and can impair extinction of conditioned fear (Ressler et al., 2011; Johnson et al., 2020). In the trigeminovascular system, PAC1 receptors on second-order neurons in the trigeminocervical complex mediate delayed central sensitization after PACAP-38 exposure — an effect not replicated by VIP or by PACAP-38 acting at VPAC1/VPAC2, pointing to PAC1 as the therapeutically relevant migraine target (Rubio-Beltrán et al., 2018).

Open questions

  • Why did both Phase 2 trials targeting the PACAP-PAC1 axis (AMG 301 and LY3451838) fail to separate from placebo in migraine prevention, despite compelling human provocation data implicating PACAP-38?
  • Does the sex-specific PTSD association reflect estrogen-dependent regulation of ADCYAP1R1 expression, and would PAC1 antagonism show differential efficacy by sex in clinical anxiety or trauma trials?
  • What is the functional consequence of the avian co-localization of GHRH and PACAP on a single gene, and do co-expression patterns in chicken tissue differ meaningfully from mammalian PACAP distribution?
  • PAC1 splice-variant selectivity: can isoform-selective ligands dissociate the neuroprotective and pain-sensitizing arms of PACAP signaling?

Related peptides

  • PACAP-27 — the 27-residue N-terminal fragment of PACAP-38, arising from the same precursor via internal cleavage at Gly28–Lys29–Arg30; shares identical potency at PAC1 but lacks the C-terminal 11 residues present in PACAP-38
  • VIP (vasoactive intestinal peptide) — closest structural relative; acts at VPAC1 and VPAC2 but has roughly 100-fold lower affinity for PAC1 than PACAP-38, making it the key contrast peptide for isolating PAC1-specific biology in pharmacological experiments
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 2026-06-05

Could PACAP-38 cause migraines through VPAC receptors instead of PAC1R?

If true, new migraine drugs could target VPAC1 or VPAC2 instead of PAC1R, potentially helping patients who do not respond to current PAC1R-blocking therapies. This would redirect years of drug development toward a more precise target.

The hypothesis
PACAP-38 binds VPAC1/VPAC2 with comparable or higher affinity than PAC1R in certain tissues, and tissue-selective migraine phenotypes may reflect which receptor dominates rather than PAC1R alone.
Why it’s plausible
PACAP-38 is annotated only for PAC1R, yet it is a member of the secretin/VIP family and literature shows PACAP can activate VPAC receptors. The openfold3-mlx/complex prediction shows moderate interface confidence (ipTM=0.762) and low pLDDT (41.5), suggesting the modeled PAC1R interface may be uncertain or partially disordered. If PACAP-38 has been evolutionarily constrained across vertebrates for broad receptor engagement, migraine-related phenotypes (vasodilation, neurogenic inflammation) could be driven by VPAC1/VPAC2 in vascular endothelium rather than neuronal PAC1R.
Why it matters
If true, therapeutic strategies that only antagonize PAC1R may incompletely block PACAP-driven migraine mechanisms, and dual or VPAC-selective modulation could be more effective.
Plausibility.85
Novelty.40
Impact.80
Basis · grounding2 computed/notes
[1]
structureopenfold3-mlx/complex ipTM=0.762, pLDDT=41.5 against PAC1R suggests moderate/uncertain interface confidence, leaving room for alternative or additional receptors
[2]
notePACAP-38 belongs to the secretin/glucagon/VIP peptide family and was identified by cAMP stimulation in pituitary cells; the shorter PACAP-27 variant arises from the same precursor
openupdated 2026-06-05

Could PACAP-38 change how immune cells in the brain behave, not just nerve cells?

If true, PACAP-38 could be tested for diseases like multiple sclerosis or brain injury where overactive immune cells cause damage, giving an old peptide new jobs beyond pain and migraine.

The hypothesis
PACAP-38, originally annotated for pituitary cAMP activation, also modulates immune cell metabolism through PAC1R expressed on macrophages and microglia, and could be repurposed from a neuromodulator to an immunometabolic therapy for neuroinflammatory conditions.
Why it’s plausible
PACAP-38 was discovered by its ability to stimulate cAMP in pituitary cells, but cAMP is also a master regulator of macrophage polarization and microglial activation. If PAC1R is expressed on CNS-resident immune cells, PACAP-38 could shift microglia from pro-inflammatory M1-like to reparative M2-like states. The peptide's evolutionary conservation and broad tissue distribution support pleiotropic roles beyond the pituitary.
Why it matters
If true, PACAP-38 or analogs could be explored for multiple sclerosis, traumatic brain injury, or neurodegenerative diseases where microglial dysregulation drives pathology, expanding the therapeutic scope beyond pain and migraine.
Plausibility.75
Novelty.45
Impact.70
Basis · grounding2 computed/notes
[1]
notePACAP-38 was identified by its ability to stimulate cyclic AMP production in pituitary cells; cAMP is a universal second messenger also controlling immune cell metabolism
[2]
notePACAP-38 is found in the nervous system of virtually all vertebrates, suggesting broad tissue roles beyond the pituitary
openupdated 2026-06-05

Could the starting histidine make PACAP-38 more active in acidic, inflamed areas like the brain during a migraine?

If true, scientists could design PACAP drugs that turn on only where tissue is inflamed, reducing side effects in healthy parts of the body and making treatments safer and more precise.

The hypothesis
The N-terminal histidine of PACAP-38 (position 1) acts as a pH-sensitive conformational switch that modulates receptor affinity in acidic tissue microenvironments such as inflamed meninges or ischemic brain tissue.
Why it’s plausible
PACAP-38 begins with His-Ile-Asp-Gly. Histidine has a side-chain pKa near 6.0, making it uniquely sensitive to pH shifts in pathological tissues. If protonation of H1 alters the N-terminal helix dipole or receptor docking, PACAP-38 could have higher activity at sites of inflammation or ischemia where pH drops, effectively targeting itself to diseased tissue.
Why it matters
If true, PACAP-38 analogs could be engineered to sharpen or blunt this pH sensitivity, creating inflammation-seeking or inflammation-avoiding variants for targeted migraine or stroke therapy.
Plausibility.55
Novelty.75
Impact.65
Basis · grounding2 computed/notes
[1]
sequenceN-terminus HIDGIFT... places histidine at position 1, a residue with pKa ~6.0 that changes charge across physiological/pathological pH ranges
[2]
notePACAP-38 is linked to pain and migraine, conditions associated with tissue acidosis and inflammatory pH shifts
openupdated 2026-06-05

Could short bursts of PACAP-38 protect brain cells while long-term exposure causes migraines?

If true, doctors could use PACAP-38 to protect the brain after a stroke or injury, but only for a short time, and avoid chronic use that might trigger or worsen headaches. This would clarify when the peptide helps versus harms.

The hypothesis
PACAP-38 acts as a bidirectional stress switch: acute release promotes neuroprotection via PAC1R-cAMP signaling, while chronic elevation drives neurogenic inflammation and migraine sensitization through receptor desensitization or PAC1R splice-variant bias.
Why it’s plausible
PACAP-38 is linked to stress, pain, and migraine. The literature notes PAC1R exists as 467 or 495 amino acid splice variants generated by alternative splicing. If different splice variants couple differently to cAMP versus other pathways, acute versus chronic PACAP-38 exposure could shift the signaling balance from protective to pro-inflammatory.
Why it matters
If true, the therapeutic window for PACAP-based neuroprotection is narrow, and timing or route of administration would determine whether the peptide helps or harms in neurodegenerative or headache conditions.
Plausibility.60
Novelty.55
Impact.75
Basis · grounding1 paper · 1 computed/note
[1]
paper
PACAP Type I receptor consists of 467 or 495 amino acids, difference generated by alternative splicing, suggesting isoform-specific functions
doi: 10.1006/bbrc.1993.2423
[2]
notePACAP-38 is a brain signaling peptide linked to stress, pain, and migraine
openupdated 2026-06-05

Could the missing C-terminal amide make PACAP-38 break down faster while still working fine?

If true, doctors could adjust whether a synthetic version includes that tag based on whether they need a short burst or a long-lasting effect, making treatments more flexible and possibly cheaper to produce.

The hypothesis
The C-terminal amide of PACAP-38, absent in the stored raw sequence, is required for stability against carboxypeptidases in plasma but dispensable for receptor activation, creating a natural trade-off between half-life and potency.
Why it’s plausible
The readme states native PACAP-38 carries a C-terminal amide not represented in the raw stored sequence, and that this modification is not required for PAC1R activation (Bourgault et al., 2016). If the unamidated form is still active but more rapidly degraded, this could explain why the 38-residue form dominates in vivo despite the shorter PACAP-27 variant: the extra C-terminal residues plus amidation protect against exopeptidase trimming.
Why it matters
Understanding the exact structural determinants of stability versus activity would guide whether therapeutic analogs should preserve amidation for durability or omit it for simpler recombinant manufacturing.
Plausibility.70
Novelty.50
Impact.60
Basis · grounding2 computed/notes
[1]
sourceBourgault et al., 2016: C-terminal amide is not required for PAC1 receptor activation
[2]
sequence38-residue sequence HIDGIFTDSYSRYRKQMAVKKYLAAVLGKRYKQRVKNK terminates in free carboxylate in stored form, lacking the native C-terminal amidation
details expand to inspect
full evidence table2 metrics
metricvaluetool
ipTM 0.76238614320755 openfold3-mlx
ranking score 0.8443729877471924 openfold3-mlx
structural qualityopenfold3
0
metricvaluenote
gpde0.836global PDE — lower = better
disorder0.190fraction disordered
chain pair ipTM (A, B)0.762interface quality
3-letter notation
His-Ile-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-Lys-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
runtime450s
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 signaling peptide linked to stress, pain, and migraine (pep-10581, v1). PeptideModel. https://peptidemodel.com/card/pep-10581
@peptide{pep10581,
  sequence = {HIDGIFTDSYSRYRKQMAVKKYLAAVLGKRYKQRVKNK},
  target   = {pac1r},
  author   = {peptidemodel},
  year     = {2026},
  status   = {synthesized}
}
related peptides 5 by signal overlap
clinical trials 5 on ct.gov · checked 2026-05-09
ct.gov trials 5
PubMed RCT 1
by phase
5no phase
by status
4completed1recruiting
references 8 papers
[8] supporting
discussion no comments
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