pe
pep-10650 v1 CC-BY-SA-4.0

Stress-response trigger hormone (CRF/CRH)

Natural brain hormone that starts the body's stress response by signaling the pituitary to release cortisol-triggering hormones; a research tool used to study stress, anxiety, and the adrenal system.

statussynthesized targetCRHR2 length41 aa refs3
status 4 / 5
prediction metrics openfold3-mlx 0.3.1
ipTM0.800
pTM0.725
avg pLDDT53.1
ranking score0.871
STRUCTURE · PEP-10650 × CRHR2
ranking0.871
target interface 4.5Å peptide drag rotate · ctrl+scroll zoom · right-click pan
openfold3-mlx 0.3.1 · mmCIF ↓ download
sequence41 aa
151015202530354041
SEEPPISLDLTFHL LREVLEMARAEQLA QQAHSNRKLMEII
overview readme

What this is

Corticotropin-releasing factor (CRF), also called corticotropin-releasing hormone (CRH), is a 41-amino-acid neuropeptide released by neurons in the hypothalamus. It is the master switch that starts the body's stress response: when the brain perceives a threat, CRF is secreted into the small portal vessels feeding the pituitary, where it tells the pituitary to release ACTH, which in turn signals the adrenal glands to make cortisol. The stored sequence here is the human/rat form (identical between the two species), which is C-terminally amidated (ends in -Ile-NH₂) — that amide is not visible in the raw one-letter sequence but is essential for receptor binding and circulating stability. CRF was the first piece of the hypothalamus-pituitary-adrenal (HPA) axis to be molecularly identified, and remains one of the most studied neuropeptides in the brain.

History

The existence of a hypothalamic factor that drives ACTH release was hypothesized in 1955 by Guillemin & Rosenberg and by Saffran & Schally, but it took more than 25 years to isolate it. The 41-residue peptide was finally characterized in 1981 by Wylie Vale, Joachim Spiess, Catherine Rivier, and Jean Rivier at the Salk Institute, who purified it from sheep hypothalamic extracts and reported the primary structure in Science (Vale et al., 1981). The human and rat forms — which differ from the ovine sequence at seven positions — were identified shortly thereafter and are identical to each other. CRF is now recognized as the prototypical member of a four-peptide family that also includes urocortin 1, urocortin 2, and urocortin 3 (Bale & Vale, Annu. Rev. Pharmacol. Toxicol., 2004).

What it does

CRF acts on two class B G-protein-coupled receptors, CRF receptor 1 (CRHR1) and CRF receptor 2 (CRHR2). Native CRF binds CRHR1 with roughly 10-fold higher affinity than CRHR2, so most of its physiological actions are CRHR1-driven (Bale & Vale, 2004). At the pituitary, CRHR1 activation triggers cAMP-mediated release of ACTH from corticotrophs, which is the classical endocrine arm of the stress response. In the brain — particularly the amygdala, locus coeruleus, and bed nucleus of the stria terminalis — CRF acts as a neuromodulator rather than a hormone, producing the behavioural side of the stress reaction: increased arousal, vigilance, anxiety-like behaviour, and suppression of feeding and reproductive drives (Ohmura et al., CNS Neurol. Disord. Drug Targets, 2009; Reul & Holsboer, Curr. Opin. Pharmacol., 2002). The CRHR2 system, by contrast, is preferentially engaged by urocortin 2 and urocortin 3 and appears to participate in dampening and resolving the stress response.

Evidence

  • Human: Synthetic CRF (the human/rat sequence and the ovine sequence as a separate product) is used clinically as a diagnostic tool — the "CRH stimulation test" — to distinguish pituitary Cushing's disease from ectopic ACTH-secreting tumours and to investigate adrenal insufficiency. Ovine CRF has higher diagnostic sensitivity than human/rat CRF for Cushing's disease, attributed to slower clearance (Nieman et al., J. Clin. Endocrinol. Metab., 1989). The HPA-axis abnormalities seen in major depression and post-traumatic stress disorder are widely interpreted as CRF-system dysregulation (Reul & Holsboer, 2002; Jiang et al., Front. Cell. Neurosci., 2019).
  • Animal: Central (intracerebroventricular) CRF injection in rodents reproduces a stress-like behavioural profile — heightened anxiety, reduced food intake, autonomic activation — that is reversed by CRHR1 antagonists. CRHR1 knockout mice show blunted HPA responses and reduced anxiety-like behaviour, while CRHR2 knockouts show the opposite tendency, supporting opposing roles for the two receptors (Bale & Vale, 2004).
  • In vitro: Cultured anterior pituitary cells release ACTH and β-endorphin in response to CRF; this was the bioassay used in the original Vale isolation work (Vale et al., 1981).

Known effects

  • Pituitary ACTH release — Mechanistically established; the basis of the clinical CRH stimulation test (Vale et al., 1981).
  • Anxiety- and stress-like behaviour (central administration in animals) — Robust preclinical effect at CRHR1 (Ohmura 2009; Bale & Vale 2004).
  • Appetite suppression — Preclinical; central CRF reduces food intake.
  • Mood and HPA-axis dysregulation in depression — Strong correlative human evidence; CRF hyperactivity is one of the most reproducible biological findings in major depression (Reul & Holsboer 2002; Jiang 2019).

Safety signals

The clinical CRH stimulation test, in which a small intravenous dose of synthetic CRF is given, is generally well tolerated; the most commonly reported transient effects are facial flushing and a brief feeling of warmth or shortness of breath, consistent with a known vasodilatory action (Nieman 1989). Outside this narrow diagnostic indication, CRF itself is not used therapeutically. Drug-development efforts have focused on small-molecule CRHR1 antagonists (e.g. pexacerfont, verucerfont, GSK561679) for stress-related psychiatric disorders; despite a clean preclinical rationale, these have largely failed to demonstrate efficacy in clinical trials for depression, generalized anxiety disorder, or alcohol craving (Kwako et al., Neuropsychopharmacology, 2015).

Regulatory status

  • US: Synthetic human CRF (corticorelin, ovine sequence under the brand name Acthrel) is FDA-approved as a diagnostic agent for distinguishing pituitary versus ectopic causes of ACTH-dependent Cushing's syndrome. It is not approved for any therapeutic indication.
  • EU: Synthetic CRF is similarly available in several jurisdictions as a diagnostic peptide for the CRH stimulation test; it is not an approved therapy.
  • WADA: CRF and its receptor-active analogs fall under S2 (peptide hormones, growth factors, related substances and mimetics) of the WADA Prohibited List by virtue of being a corticotropin-releasing factor that drives endogenous ACTH and cortisol.

Related peptides

CRF is the founding member of a four-peptide mammalian family that also includes urocortin 1 (binds both CRHR1 and CRHR2), urocortin 2 (CRHR2-selective), and urocortin 3 (CRHR2-selective). The urocortins are the peptides typically used experimentally when investigators want to engage CRHR2 selectively, in contrast to CRF's CRHR1 preference (Bale & Vale, 2004).

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

Is the chemical modification at the very tip of this stress hormone doing active receptor-binding work, not just protecting the molecule from degradation?

If the amide cap is a genuine binding element, chemists could copy or improve it to make more effective and longer-lasting drugs for conditions driven by the stress hormone system, including anxiety, PTSD, and Cushing's disease.

The hypothesis
The C-terminal amidation of CRF 1-41 (Ile41-NH2, not visible in the stored sequence) is not merely a stability modification but is a structural determinant that reorients the C-terminal helix to increase the electrostatic complementarity with the CRHR1 extracellular domain, and its absence converts CRF into a partial agonist.
Why it’s plausible
Class B GPCR ligands depend critically on C-terminal modifications for receptor engagement. The readme explicitly notes the C-terminal amide is essential for receptor binding and stability. Amidation neutralizes the terminal carboxylate, altering the local electrostatic environment and potentially the helical cap conformation. If the amide directly contacts a charged residue in the CRHR1 ECD, its removal would reduce binding energy and Emax, converting the peptide from full to partial agonist rather than simply destabilizing it.
Why it matters
If C-terminal amidation is a structural pharmacophore element rather than a passive stability feature, it becomes a rational design handle: synthetic amide bioisosteres could yield protease-resistant CRF analogs that retain full agonism at CRHR1.
Plausibility.65
Novelty.55
Impact.60
Basis · grounding3 computed/notes
[1]
noteC-terminal amidation (Ile-NH2) described as essential for receptor binding and circulating stability; amide is not visible in the raw sequence
[2]
sequenceSequence ends in ...KLMEII; position 41 is Ile, the site of amidation; the raw sequence cannot encode the amide, masking this pharmacophoric element
[3]
structurepLDDT=53.1 at C-terminus consistent with a disordered or poorly modeled C-terminal region in the absence of amide information, supporting the idea that amide geometry changes the C-terminal pose
openupdated 2026-06-05

Do the handful of amino-acid differences between human and sheep CRF explain why human CRF targets mainly the anxiety-driving stress receptor while the sheep version is less choosy?

Mapping these differences would give scientists a precise recipe for engineering synthetic stress hormones that activate only the desired receptor, accelerating the development of more targeted treatments for stress, anxiety, and HPA-axis disorders.

The hypothesis
The seven sequence positions where human/rat CRF differs from ovine CRF cluster on one face of the predicted amphipathic helix and collectively reduce CRHR2 affinity relative to CRHR1, explaining why human CRF is primarily a CRHR1 agonist while ovine CRF retains broader dual-receptor activity.
Why it’s plausible
Human and rat CRF differ from the ovine sequence at seven positions; the human/rat form has been identified as more CRHR1-selective. If these seven differences are non-random and map to the receptor-contact face rather than the solvent-exposed face of the central helix, they would explain subtype selectivity as a simple biophysical property of the amphipathic surface, rather than a complex allosteric phenomenon.
Why it matters
A structure-function map of the seven ovine-to-human substitutions would provide a rational basis for engineering human-CRF-like peptides with tunable CRHR1/CRHR2 selectivity without moving to fully synthetic analogs.
Plausibility.65
Novelty.55
Impact.60
Basis · grounding3 computed/notes
[1]
noteHuman and rat CRF differ from ovine CRF at seven positions; the four-member CRF family includes CRF, urocortin 1, 2, and 3 with distinct receptor selectivities
[2]
sequence41-aa sequence SEEPPISLDLTFHLLREVLEMARAEQLAQQAHSNRKLMEII; helical regions can be predicted from the known CRF structure to identify contact versus solvent faces
[3]
structurepLDDT=53.1 consistent with partially ordered helix; low confidence may reflect the seven-position difference from ovine sequences used to train folding models
openupdated 2026-06-05

Is the stress hormone CRF actually better matched to the anxiety-driving receptor than the recovery receptor it has been labeled as targeting?

Getting the target annotation right matters for every research study that builds on it. A correction here could prevent misinterpretation of hundreds of experiments linking CRF to stress disorders, depression, and anxiety.

The hypothesis
The annotated target of human/rat CRF (CRHR2) is incorrect or incomplete: the ipTM of 0.800 at CRHR2 is lower than expected for a high-affinity endogenous agonist at its cognate receptor, and CRF 1-41 may engage CRHR1 with higher structural confidence, with CRHR2 as a secondary or lower-affinity target under physiological conditions.
Why it’s plausible
Human/rat CRF is the endogenous ligand for CRHR1 in the pituitary (the primary HPA-axis receptor) and has secondary activity at CRHR2. The readme notes it is the master stress-switch acting through CRHR1-driven ACTH release. An ipTM of 0.800 for a predicted complex with CRHR2 is moderate and does not indicate the tight binding expected of a primary endogenous agonist. The annotation may reflect CRHR2 cross-reactivity rather than primary activity, or the structure prediction docked the peptide against CRHR2 when CRHR1 would yield a higher-confidence complex.
Why it matters
Correcting the primary target annotation of the most studied neuropeptide in the brain would affect how researchers interpret CRF pharmacology studies that rely on database annotations, and clarify which receptor drives which pathological phenotype.
Plausibility.70
Novelty.50
Impact.55
Basis · grounding3 computed/notes
[1]
structureopenfold3-mlx ipTM=0.800, unexpectedly moderate for an endogenous agonist at its primary receptor; raises the question of whether CRHR2 is truly the primary target
[2]
noteCRF acts on the pituitary to release ACTH, which is CRHR1-mediated; the readme calls CRF 'the master switch' for stress but annotates CRHR2 as target
[3]
sequence41-aa human/rat CRF SEEPPISLDLTFHLLREVLEMARAEQLAQQAHSNRKLMEII is the canonical CRHR1 agonist sequence; CRHR2 selectivity is a property of analogs, not the native peptide
openupdated 2026-06-05

Does the stress hormone CRF trigger the brain's own immune cells to eliminate the protective insulating cells that are missing in depressed patients' brains?

If stress hormones directly trigger brain inflammation, anti-CRF drugs could protect brain structure in psychiatric patients, a completely new way of thinking about and treating depression and bipolar disorder that goes beyond adjusting mood-related chemical signals.

The hypothesis
CRF 1-41 activates CRHR1 expressed on microglia and drives a neuroinflammatory phenotype that contributes to white-matter pathology in mood disorders, and this neuroimmune CRF-CRHR1 axis is pharmacologically distinct from the HPA-axis CRF-CRHR1 axis and accessible to CNS-penetrant CRHR1 antagonists.
Why it’s plausible
Microglial CRHR1 expression has been reported; microglia activated by stress-related signals contribute to oligodendrocyte death. The documented glial loss in depressed amygdala (10.3389/fncel.2019.00290) may reflect microglial-mediated oligodendrocyte elimination downstream of CRF-driven CRHR1 activation. This pathway would be independent of the pituitary CRF-ACTH axis, meaning HPA-axis normalization alone would not prevent brain glial damage.
Why it matters
Recognizing a central neuroimmune CRF-CRHR1 axis would change the target profile for next-generation CRF antagonists, favoring CNS-penetrant, brain-selective compounds over peripherally acting ones, and would link stress-biology to neuroimmunology in mood disorders.
Plausibility.50
Novelty.60
Impact.65
Basis · grounding1 paper · 1 computed/note
[1]
paper
Oligodendrocyte and glial loss in limbic regions of mood disorder patients; inflammatory mechanisms are implicated in white-matter pathology
doi: 10.3389/fncel.2019.00290
[2]
noteCRF 1-41 is the endogenous CRHR1 agonist; CRHR1 is expressed in multiple brain cell types beyond the pituitary corticotrophs
openupdated 2026-06-05

Does the brain's main stress hormone, when overactive for too long, destroy the insulating cells in emotional brain regions, and could blocking it stop that damage?

If this mechanism is confirmed, doctors might be able to identify depressed patients with brain-cell damage using brain imaging, then treat them with CRF receptor blockers to prevent further damage, a precision approach that could help the roughly 30% of patients who do not respond to current antidepressants.

The hypothesis
Chronic CRF hypersecretion in depression drives oligodendrocyte loss in the amygdala via CRHR1 activation, and CRHR1 antagonism in limbic white matter, not just in the pituitary, represents an underexplored mechanism by which CRF antagonists produce antidepressant effects.
Why it’s plausible
The literature snippet (10.3389/fncel.2019.00290) documents oligodendrocyte and total glial cell reduction in the amygdala of depressed patients. CRF is the master stress activator, and prolonged CRHR1 activation has pro-inflammatory and pro-apoptotic effects on glia. If stress-driven CRF excess selectively kills oligodendrocytes in limbic white matter, CRHR1 antagonists would reduce this damage independent of their HPA-axis effects. Clinical CRHR1 antagonist trials have shown modest antidepressant effects; a glial protection mechanism could explain why.
Why it matters
Identifying oligodendrocyte protection as a therapeutic mechanism for CRHR1 antagonists would redirect drug development toward CNS biomarkers (white-matter imaging, glial markers) and patient populations with stress-driven mood disorders and measurable white-matter pathology.
Plausibility.45
Novelty.60
Impact.70
Basis · grounding1 paper · 2 computed/notes
[1]
paper
Reduction in glial cells and oligodendrocytes in amygdala of depressed, bipolar, and schizophrenic patients; stress-axis overactivation is a documented feature of these conditions
doi: 10.3389/fncel.2019.00290
[2]
noteCRF is the master switch for the stress response; chronic CRF excess is implicated in major depression and anxiety disorders
[3]
sequenceCRF 1-41 is the endogenous full agonist driving CRHR1 in pituitary and CNS, providing mechanistic link between CRF excess and downstream glial effects
details expand to inspect
full evidence table2 metrics
metricvaluetool
ipTM 0.800086498260498 openfold3-mlx
ranking score 0.8714042901992798 openfold3-mlx
structural qualityopenfold3
0
metricvaluenote
gpde0.709global PDE — lower = better
disorder0.173fraction disordered
chain pair ipTM (A, B)0.800interface quality
3-letter notation
Ser-Glu-Glu-Pro-Pro-Ile-Ser-Leu-Asp-Leu-Thr-Phe-His-Leu-Leu-Arg-Glu-Val-Leu-Glu-Met-Ala-Arg-Ala-Glu-Gln-Leu-Ala-Gln-Gln-Ala-His-Ser-Asn-Arg-Lys-Leu-Met-Glu-Ile-Ile
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
runtime350s
predicted bymlx@peptide
predicted at2026-04-22
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). Stress-response trigger hormone (CRF/CRH) (pep-10650, v1). PeptideModel. https://peptidemodel.com/card/pep-10650
@peptide{pep10650,
  sequence = {SEEPPISLDLTFHLLREVLEMARAEQLAQQAHSNRKLMEII},
  target   = {crhr2},
  author   = {peptidemodel},
  year     = {2026},
  status   = {synthesized}
}
related peptides 4 by signal overlap
clinical trials 527 on ct.gov · 16 on EUCTR · checked 2026-05-22
ct.gov trials 527
with results 172
EUCTR 16
PubMed reviews 2
by phase
1phase 14phase 22phase 32phase 41early phase 12no phase
by status
4completed1recruiting2terminated3unknown
references 3 papers
discussion no comments
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