Compound monograph

Sermorelin

Sermorelin is the synthetic peptide corresponding to residues 1 to 29 of human growth hormone-releasing factor, the unmodified parent fragment from which several longer-acting analogs are derived.

Published: 2026-09-04Last updated: 2026-10-14Literature/identifier verification: 2026-08-23

Also known asGRF(1-29)SermorelinaSermorelinum

GHRH analogs

Identity & nomenclature

Sermorelin is the synthetic peptide corresponding to residues 1 to 29 of human growth hormone-releasing factor, the unmodified parent fragment from which several longer-acting analogs are derived.

Sermorelin corresponds to residues 1 to 29 of human growth hormone-releasing factor, the fragment commonly written GRF(1-29). Two related entries are in this library. CJC-1295 is a tetrasubstituted analog of this fragment; the form bearing an added C-terminal maleimidopropionamide lysine, which enables albumin conjugation, is a separate species from the one the CJC-1295 entry describes. Tesamorelin is not a derivative of the fragment: it is the full 44-residue sequence, of which this fragment is the first 29 residues, carrying an N-terminal hexenoyl group and a C-terminal amide.

Declared aliases and development codes: GRF(1-29), Sermorelina, Sermorelinum.

Molecular properties

Molecular formula	C149H246N44O42S
Molecular mass	3357.9 Da
CAS Registry Number	86168-78-7
PubChem CID	16132413
UNII	89243S03TE
One-letter sequence	YADAIFTNSYRKVLGQLSARKLLQDIMSR
Three-letter sequence	Tyr–Ala–Asp–Ala–Ile–Phe–Thr–Asn–Ser–Tyr–Arg–Lys–Val–Leu–Gly–Gln–Leu–Ser–Ala–Arg–Lys–Leu–Leu–Gln–Asp–Ile–Met–Ser–Arg
Terminal groups	Free N-terminus; C-terminal amide at Arg29

The N-terminal 29 residues of human growth hormone-releasing hormone, carried as a C-terminal amide. The recorded molecular formula and mass are the values this sequence derives with that amide applied; without it the derivation gives the free acid and does not match. The IUPHAR/BPS Guide to Pharmacology (ligand 6998, release 2026.3.1) prints a thirty-residue sermorelin sequence ending Gln30; this record keeps the twenty-nine-residue fragment ending in Arg29 amide, matching PubChem CID 16132413.

Structural characteristics

Sermorelin is the unmodified GRF(1-29) fragment. The cited report synthesised three maleimido derivatives of hGRF(1-29) and bioconjugated them to human serum albumin; all three showed enhanced in vitro stability against dipeptidyl peptidase IV relative to the unmodified fragment, and were active in a growth hormone secretion assay in cultured rat anterior pituitary cells. That study was designed to identify CJC-1295, not to characterise sermorelin: unmodified hGRF(1-29) appears in it as the comparator against which the conjugates were measured. It is cited here for what it shows about the fragment, not as a characterisation of sermorelin in its own right.

Terminal features: Free N-terminus, C-terminal amide at Arg29.

Molecular targets & mechanisms

GHRH receptor

GHRHR · Growth hormone-releasing hormone receptor

A class B G-protein-coupled receptor expressed on anterior pituitary somatotrophs. Synthetic growth hormone-releasing factor analogs are characterized by their activity at this receptor.

Analytical considerations

The single sulfur atom corresponds to the methionine at position 27, the only sulfur-containing residue in the recorded sequence, and is relevant to oxidation-related degradation. Sermorelin and tesamorelin have identical residues at positions 1 to 29, so a comparison that establishes only that shared residue sequence does not show which of the two is present; they differ in chain length, in tesamorelin's N-terminal hexenoyl group and in the position of the C-terminal amide, and mass-based identity methods distinguish them directly. CJC-1295 differs from this sequence at four positions, which are recorded on its entry.

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.

Sources disagree · this Library follows one source · Residue count
Sermorelin's length in the Guide to Pharmacology
Often mixed up · Name or substance
Sermorelin and tesamorelin share residues 1 to 29

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

Rat anterior pituitary primary cells
In rat anterior pituitary primary cells, the study reported growth hormone release with hpGRF-29 and a minimal effective concentration of 0.4 × 10^-15 M.
Reference [3]
Rat anterior pituitary primary cells
In rat anterior pituitary primary cells, the study observed no stimulation of LH, FSH or PRL by hpGRF-29.
Reference [3]

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
Human growth hormone-releasing factor (hGRF)1-29-albumin bioconjugates activate the GRF receptor on the anterior pituitary in rats: identification of CJC-1295 as a long-lasting GRF analog.
Jetté L, Léger R, Thibaudeau K, Benquet C, Robitaille M, Pellerin I, Paradis V, van Wyk P, Pham K, Bridon DP
Endocrinology · 2005-04-07 · Journal Article
current
PMID 15817669 DOI 10.1210/en.2004-1286 CJC-1295 Sermorelin GHRHR
Reference 2
PEGylation of growth hormone-releasing hormone (GRF) analogues.
Esposito P, Barbero L, Caccia P, Caliceti P, D'Antonio M, Piquet G, Veronese FM
Advanced drug delivery reviews · 2003-09-26 · Review
current
PMID 14499707 DOI 10.1016/s0169-409x(03)00109-1 Sermorelin
Reference 3
An extremely sensitive in vitro model for elucidating structure-activity relationships of growth hormone-releasing factor analogs.
Heiman ML, Nekola MV, Murphy WA, Lance VA, Coy DH
Endocrinology · 1985-01 · Journal Article
current
PMID 2856874 DOI 10.1210/endo-116-1-410 Sermorelin

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
Jetté L et al. 2005	Study models reported: in vitro; animal (rat) · from the abstract
Esposito P et al. 2003	Review article
Heiman ML et al. 1985	Study models reported: in vitro · from the abstract

Compare

Catalog listing

Record history

Published 2026-09-04.

2026-10-14: Sequence and structure
2026-10-12: Sequence and structure
2026-10-08: Analytical notes
2026-10-06: Identity and nomenclature, Analytical notes
2026-09-20: References
2026-09-17: Sequence and structure, Analytical notes, References

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. Sermorelin. Published 2026-09-04; updated 2026-10-14. https://purelypeptides.org/research/compounds/sermorelin/

Methodology & citation verification

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