Compound monograph
Examorelin (Hexarelin)
Examorelin, widely supplied as hexarelin, is a synthetic hexapeptide growth hormone secretagogue carrying a 2-methylated D-tryptophan.
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Identity & nomenclature
Examorelin, widely supplied as hexarelin, is a synthetic hexapeptide growth hormone secretagogue carrying a 2-methylated D-tryptophan.
Examorelin and hexarelin are one substance under two names, not two entries. Its relationship to GHRP-6 is a single methyl group — a net CH2, 14.0157 Da — but 'methylated GHRP-6' is insufficient identity information unless the methyl position is retained.
Canonical name: Examorelin.
Declared aliases and development codes: Hexarelin, EP-23905, MF-6003.
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Molecular properties
| Molecular formula | C47H58N12O6 |
|---|---|
| Molecular mass | 887.06 Da |
| CAS Registry Number | 140703-51-1 |
| PubChem CID | 6918297 |
| UNII | 09QF37C617 |
| Three-letter sequence | His–2-Me-D-Trp–Ala–Trp–D-Phe–Lys |
| Terminal groups | Free N-terminus; C-terminal amide at Lys6 |
Position 2 carries a methyl group at INDOLE POSITION 2 of D-tryptophan. It is not an N-methyl and not an alpha-methyl substitution; those are different molecules with the same formula. No one-letter string is published here.
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Structural characteristics
This is the compound that refutes the assumption that synthetic secretagogues are interchangeable or GHSR-exclusive. Beyond ghrelin-receptor agonism, exact-compound work identifies CD36 as a binding target, maps the binding site to a defined fragment of the CD36 sequence, and reports that a cardiovascular response to hexarelin is absent in CD36-null animals. CD36 is a scavenger receptor, not a GHSR subtype. The relative contribution of the two targets belongs to the preparation tested, not to the compound in general.
- 2-methyl-D-tryptophan at position 2
- D-Phe5
Terminal features: Free N-terminus, C-terminal amide at Lys6.
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Molecular targets & mechanisms
Growth hormone secretagogue receptor
GHS-R1a · Ghrelin receptor · GHSR
A G-protein-coupled receptor distinct from the GHRH receptor. Antagonist profiling reported that ipamorelin releases growth hormone through a GHRP-like receptor rather than through the GHRH receptor, establishing the two pathways as separate.
CD36 scavenger receptor
CD36 · FAT · SR-B2
A multifunctional scavenger receptor, distinct from the growth hormone secretagogue receptor, reported as a binding target for certain synthetic secretagogue peptides. It is recorded separately here precisely because collapsing it into the ghrelin-receptor mechanism would erase the finding that these compounds are not pharmacologically interchangeable.
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Analytical considerations
The mass difference from GHRP-6 is readily measurable, but equal-mass methyl positional isomers and D/L variants are not resolved by mass alone; establishing the indole-2 position needs NMR or an authenticated orthogonal comparison. A positive GHSR assay is unusually weak evidence here, because the compounds it would distinguish this from were selected for sharing that activity.
Disagreements and mix-ups
Points where sources disagree about this compound's identity, or where a name or form is easily confused with another, as noted in this record. The discrepancy register quotes the passage for each one.
Often mixed up · One substance, two names
Examorelin and hexarelin: one substance, two namesOften mixed up · Name or substance
Examorelin vs "methylated GHRP-6"
What the studies reported
Each finding describes one cited study in its stated model. These observations are specific to that study and do not establish effects in other settings.
Cell and tissue studies
Isolated perfused hearts, species not specified in the abstract
In isolated perfused hearts whose species was not specified in the abstract, the study observed increased coronary perfusion pressure with hexarelin.
Reference [1]Isolated hearts from CD36-null mice
In isolated hearts from CD36-null mice, the study observed no hexarelin-associated increase in coronary perfusion pressure.
Reference [1]CD36 covalent photolabeling and cleavage assays
Using CD36 covalent photolabeling and cleavage assays, the study identified an 8 kDa fragment spanning Asn132-Glu177 as the hexarelin-binding site.
Reference [2]CD36 photoligand-receptor complex CNBr cleavage assay
Using a CD36 photoligand-receptor complex CNBr cleavage assay, the study observed free-ligand release and suggested Met169 as the ligand contact point.
Reference [2]
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Verified bibliography
Cited studies by type
The 3 papers this record cites, counted by the kind of work each reports. A count is the size of this record's selection, not of the research that exists, and says nothing about results, safety, effectiveness or approval.
A paper can report more than one kind of work. Each count opens those papers in the bibliography. Compare every record on the Evidence Map.
Reference 1
CD36 mediates the cardiovascular action of growth hormone-releasing peptides in the heart.Bodart V, Febbraio M, Demers A, McNicoll N, Pohankova P, Perreault A, Sejlitz T, Escher E, Silverstein RL, Lamontagne D, Ong H
Circulation research · 2002-05-03 · Journal Article
currentReference 2
Identification of the growth hormone-releasing peptide binding site in CD36: a photoaffinity cross-linking study.Demers A, McNicoll N, Febbraio M, Servant M, Marleau S, Silverstein R, Ong H
The Biochemical journal · 2004-09-01 · Journal Article
currentReference 3
Determination of growth hormone releasing peptides (GHRP) and their major metabolites in human urine for doping controls by means of liquid chromatography mass spectrometry.Thomas A, Höppner S, Geyer H, Schänzer W, Petrou M, Kwiatkowska D, Pokrywka A, Thevis M
Analytical and bioanalytical chemistry · 2011-02-06 · Journal Article
current
Study models of these references
What kind of experiment each cited paper reports, taken from its abstract unless marked. Not a summary of results.
| Reference | Study models |
|---|---|
| Bodart V et al. 2002 | Study models reported: in vitro · from the abstract |
| Demers A et al. 2004 | Study models reported: in vitro · from the abstract |
| Thomas A et al. 2011 | Study models reported: in vitro · from the abstract |
Record history
Published 2026-09-13.
- : Sequence and structure
Each entry names the parts of this record that changed on that date. Changes to links between records and to catalogue links are not listed. This history covers the tracked record fields; study findings are not listed here.
Cite this record: Purely Peptides Research Library. Examorelin (Hexarelin). Published 2026-09-13; updated 2026-10-15. https://purelypeptides.org/research/compounds/examorelin/
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Methodology & citation verification
Reference identity is checked against official PubMed metadata. Local deterministic receipts bind each normalized title and canonical metadata record to its verification date. Scientific values remain absent when an authoritative source has not been verified.
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