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From the body

Pepcan-12Also known as RVD-haemopressin

An endogenous haemoglobin-derived peptide, an allosteric brake on CB1 and an amplifier at CB2.

Endogenous
Level of detail

C₆₅H₁₀₅N₁₉O₁₇

CAS 1193362-76-3

Family
Endocannabinoid or related mediatorPeptide ligand
Molar mass
1,424.60 g/mol

Updated on

In plain terms

Pepcan-12, also called RVD-hemopressin, is not a hemp molecule: it is a small peptide the body makes itself from haemoglobin, mainly in the adrenal glands. Researchers are interested in it because it binds the receptors of the endocannabinoid system and tunes the activity of other molecules there, without replacing them. Human data are lacking and no usable effect is established.

Receptors and activity

Target network

CB1Negative allosteric modulatorOnly partial displacement of [3H]CP55,940 and [3H]WIN55,212-2; allosteric ternary model with α < 1, increase in the dissociation constant of [3H]CP55,940, and reduction of the agonist-induced cAMP, [35S]GTPγS binding and receptor internalisation (Bauer 2012)
  • Activates
  • Blocks or inhibits

The lower the cited value, the closer the target sits to Pepcan-12: one ring per factor of 100. A target with no measured value stays on the edge.

Where these targets live

Where each target has been found in humans, according to the cited studies. The map shows the target, not an effect of Pepcan-12.

Brain, side view
Body, front view
Blood

CB1CB1 found in 7 regions of the body

  1. Basal gangliadenseMost dense in basal ganglia outflow nuclei1
  2. CerebellumdenseVery dense in the cerebellum1
  3. HippocampusdenseVery high concentrations in the hippocampus2
  4. AmygdaladenseHigh concentrations in the amygdala2
  5. CortexpresentPresent throughout the neocortex2
  6. Adipose tissuepresentExpressed in adipose tissue3
  7. GutpresentColonic epithelium, smooth muscle and plexus4

Map sources

  1. Herkenham M et al. Cannabinoid receptor localization in brain. Proc Natl Acad Sci U S A, 1990 (new tab)
  2. Glass M et al. Cannabinoid receptors in the human brain: a detailed anatomical and quantitative autoradiographic study in the fetal, neonatal and adult human brain. Neuroscience, 1997 (new tab)
  3. Engeli S et al. Activation of the peripheral endocannabinoid system in human obesity. Diabetes, 2005 (new tab)
  4. Wright K et al. Differential expression of cannabinoid receptors in the human colon: cannabinoids promote epithelial wound healing. Gastroenterology, 2005 (new tab)

Cited values

  1. CB1Negative allosteric modulatorno measured value cited

    Only partial displacement of [3H]CP55,940 and [3H]WIN55,212-2; allosteric ternary model with α < 1, increase in the dissociation constant of [3H]CP55,940, and reduction of the agonist-induced cAMP, [35S]GTPγS binding and receptor internalisation (Bauer 2012)

  2. CB2Positive allosteric modulatorKi = 44 nM · human56 out of 100

    Petrucci et al. 2017, Sci Rep (new tab) · competitive binding against the fluorescent tracer Pepcan-F4, human CB2; Ki 44 ± 12 nM

  3. TRPV1AntagonistIC50 = 18.6 µM · human12 out of 100

    Suárez-Suárez et al. 2024, Biomolecules (new tab) · patch-clamp, currents induced by capsaicin 1 µM, HEK293 cells expressing TRPV1-GFP; concentration-response curve 1 to 50 µM

Bar length follows the measured value (Ki, Kd, EC50 or IC50), on one scale shared by every entry, from 100 µM to 0.1 nM. A target with no cited value has no bar.

Pharmacology

Pepcan-12 is a dodecapeptide derived from the alpha chain of haemoglobin, the lead compound of the pepcan family. It does not act as a classic cannabinoid receptor agonist: in 2012, radioligand displacement analysis interpreted with the allosteric ternary complex model concluded that it is a negative allosteric modulator of the CB1 receptor, confirmed by dissociation kinetics and by reduced agonist-induced cAMP, [35S]GTPγS binding and internalisation; these are the first endogenous allosteric modulators identified for this receptor (Bauer 2012). In 2017 the same group showed the opposite effect at the human CB2 receptor, where the peptide behaves as a positive allosteric modulator (Ki 44 ± 12 nM) and moves 2-arachidonoylglycerol's EC50 for cAMP inhibition from 92.1 to 12.4 nM, about eight-fold (Petrucci 2017). The adrenals are the main endocrine source of the constitutive peptide, and the liver produces more of it after ischaemia-reperfusion (Hofer 2015; Petrucci 2017). TRPV1 channel blockade was reported in 2024, but with an IC50 of 18.6 µM, far above physiological levels (Suárez-Suárez 2024). The initial 2009 reading, which made it a CB1 agonist, has since been revised (Gomes 2009). All these results come from cell models and rodents: no clinical study exists, the peptide's plasma stability is poor and it is not bioavailable to the brain (Glasmacher & Gertsch 2021).

Key sources.

History

Source
This peptide is not a hemp constituent and does not exist in the plant: it comes from cleavage of the alpha chain of haemoglobin in mammals. Immunohistochemistry places it in noradrenergic neurons, notably the locus coeruleus and the A1, A5 and A7 groups, with no staining of dopaminergic neurons, and in the chromaffin cells of the adrenal medulla; LC-MS/MS measurement finds about 40 pmol/g in non-perfused brain and 400 to 700 pmol/g in adrenal glands, which points to chromaffin cells as the likely source of the circulating fraction (Hofer 2015). Adrenalectomy indeed causes a marked loss of constitutive pepcan-12. After ischaemia-reperfusion damage the liver contains more of it, from about 100 to about 500 pmol/g, independently of the adrenals, and levels also rise in experimental endotoxaemia (Petrucci 2017). In human plasma, measured concentrations are in the low nanomolar range (Bauer 2012).

Biosynthetic pathway

In vivo

Pepcan-12 arises from proteolysis of the alpha chain of haemoglobin, not from a terpenophenolic pathway. Pepcan-23, a longer peptide carrying the same sequence, acts as a pro-peptide: it releases pepcan-12 by shortening of its N-terminus, a conversion observed in human whole blood, in mouse adrenal gland and liver homogenates, and after administration in mice; pepcan-23 is also the most stable form in plasma (about 50 pmol/mL in human whole blood) and efficiently complexes divalent metal ions, in particular copper(II) and nickel(II), which may regulate this process (Glasmacher & Gertsch 2021).

Classification

Family, origin and source verification

Family

Endocannabinoid or related mediator › Peptide ligand

Verification

Every fact on this entry was checked against its primary sources on 20 October 2026.

Wikipedia (English)

No dedicated article.

References

  1. Bauer et al. 2012, J Biol Chem: identification of the pepcan family and negative allosteric modulation of CB1 (new tab)PMID 22952224
  2. Petrucci et al. 2017, Sci Rep: pepcan-12 (RVD-haemopressin), a positive allosteric modulator of CB2 secreted by the adrenal glands and by the injured liver (new tab)PMID 28842619
  3. Hofer et al. 2015, Neuropharmacology: localisation and production of peptide endocannabinoids in the CNS and the adrenal medulla (new tab)PMID 25839900
  4. Glasmacher & Gertsch 2021, Adv Biol Regul: pepcan-23, the propeptide of RVD-haemopressin, and stability of haemopressins in the mouse (new tab)PMID 33799079
  5. Suárez-Suárez et al. 2024, Biomolecules: RVD-haemopressin blocks the TRPV1 channel (IC50 18.6 µM) (new tab)PMID 39334900
  6. Gomes et al. 2009, FASEB J: novel endogenous peptide agonists of cannabinoid receptors (initial reading) (new tab)PMID 19380512
  7. PubChem CID 90488874, RVD-Hpalpha (new tab)

Identifiers

Names

Common name
Pepcan-12 (RVD-haemopressin)
Other names
RVD-hemopressin · RVD-Hpα · Pepcan-12 · RVDPVNFKLLSH

Identifiers

Formula
C₆₅H₁₀₅N₁₉O₁₇
CAS
1193362-76-3
PubChem CID
90488874(new tab)
InChIKey
CSDQEWILNKOWRN-WSDCEOHFSA-N
SMILES
CC(C)C[C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC1=CN=CN1)C(=O)O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC2=CC=CC=C2)NC(=O)[C@H](CC(=O)N)NC(=O)[C@H](C(C)C)NC(=O)[C@@H]3CCCN3C(=O)[C@H](CC(=O)O)NC(=O)[C@H](C(C)C)NC(=O)[C@H](CCCN=C(N)N)N

Machine-readable entry (JSON)

LLM ingestion format: a structured superset of the entry (identifiers, binding, versioned legal status). Full corpus.