Growth hormone–releasing hormone analogs

Growth hormone–releasing hormone (GHRH) is a 44-residue peptide amide. Synthetic work on it has concentrated on its first 29 residues, the shortest fragment reported to keep full activity in receptor assays, and on substitutions that slow its enzymatic cleavage. The entries here are the full-length peptide and analogs built on it; the comparison below shows exactly where each one differs from GHRH(1–44).

Members compared

Calculated from each structure

Peptide	Residues	Formula	Monoisotopic mass (Da)	Charge, pH 7	pI	Termini
CJC-1295 (no DAC)	29	C152H252N44O42	3,365.8936	4.0	10.95	free amine; amide
Sermorelin	29	C149H246N44O42S	3,355.8187	4.0	10.95	free amine; amide
GHRH (1–44) amide	44	C215H358N72O66S	5,036.6591	5.0	11.43	free amine; amide
Tesamorelin	44	C221H366N72O67S	5,132.7166	4.0	11.43	N-(trans-3-hexenoyl); amide

Sequences and relationships

Each member's sequence in three-letter code, and how it relates to GHRH (1–44) amide, worked out position by position from the structures. Members with no entry in the last column are not direct sequence relatives of GHRH (1–44) amide.

Relationship to GHRH (1–44) amide

Peptide	Sequence	Relationship
CJC-1295 (no DAC)	H-Tyr-D-Ala-Asp-Ala-Ile-Phe-Thr-Gln-Ser-Tyr-Arg-Lys-Val-Leu-Ala-Gln-Leu-Ser-Ala-Arg-Lys-Leu-Leu-Gln-Asp-Ile-Leu-Ser-Arg-NH2	Residues 1–29 of GHRH (1–44) amide, with 4 substitutions: Ala2→D-Ala, Asn8→Gln, Gly15→Ala, Met27→Leu
Sermorelin	H-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-NH2	Residues 1–29 of GHRH (1–44) amide
GHRH (1–44) amide	H-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-Gln-Gln-Gly-Glu-Ser-Asn-Gln-Glu-Arg-Gly-Ala-Arg-Ala-Arg-Leu-NH2	Reference sequence
Tesamorelin	Hexenoyl-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-Gln-Gln-Gly-Glu-Ser-Asn-Gln-Glu-Arg-Gly-Ala-Arg-Ala-Arg-Leu-NH2	Residues 1–44 of GHRH (1–44) amide; N-terminus N-(trans-3-hexenoyl) (reference: free amine)

Shared analytical features

The sequence-specific variants from each member's entry, counted across the family: what an HPLC or mass spectrometry result for these peptides is most often read against.

Variants by number of members

Variant	Members
C-terminal amide	4 of 4: CJC-1295 (no DAC), Sermorelin, GHRH (1–44) amide, Tesamorelin
Glutamine deamidation	4 of 4: CJC-1295 (no DAC), Sermorelin, GHRH (1–44) amide, Tesamorelin
Asparagine deamidation	3 of 4: Sermorelin, GHRH (1–44) amide, Tesamorelin
Methionine oxidation	3 of 4: Sermorelin, GHRH (1–44) amide, Tesamorelin
Stereochemistry	1 of 4: CJC-1295 (no DAC)

Every member can also carry the synthesis-related variants common to all synthetic peptides, described in How synthetic peptides are made.

Pairs compared in detail

• Sermorelin and CJC-1295 (no DAC) compared
• Sermorelin and Tesamorelin compared

Sources & Further Reading

1. Prohaska T, Irrgeher J, Benefield J, Böhlke JK, Chesson LA, Coplen TB, et al. Standard atomic weights of the elements 2021 (IUPAC Technical Report). Pure and Applied Chemistry 2022;94(5):573–600. doi:10.1515/pac-2019-0603
2. Wang M, Huang WJ, Kondev FG, Audi G, Naimi S. The AME 2020 atomic mass evaluation (II). Tables, graphs and references. Chinese Physics C 2021;45(3):030003. doi:10.1088/1674-1137/abddaf
3. Rice P, Longden I, Bleasby A. EMBOSS: the European Molecular Biology Open Software Suite. Trends in Genetics 2000;16(6):276–277. doi:10.1016/S0168-9525(00)02024-2
4. Pace CN, Vajdos F, Fee L, Grimsley G, Gray T. How to measure and predict the molar absorption coefficient of a protein. Protein Science 1995;4(11):2411–2423. doi:10.1002/pro.5560041120
5. Kyte J, Doolittle RF. A simple method for displaying the hydropathic character of a protein. Journal of Molecular Biology 1982;157(1):105–132. doi:10.1016/0022-2836(82)90515-0
6. Meija J, Coplen TB, Berglund M, Brand WA, De Bièvre P, Gröning M, et al. Isotopic compositions of the elements 2013 (IUPAC Technical Report). Pure and Applied Chemistry 2016;88(3):293–306. doi:10.1515/pac-2015-0503
7. Roepstorff P, Fohlman J. Letter to the editors: proposal for a common nomenclature for sequence ions in mass spectra of peptides. Biomedical Mass Spectrometry 1984;11(11):601. doi:10.1002/bms.1200111109
8. Biemann K. Contributions of mass spectrometry to peptide and protein structure. Biomedical and Environmental Mass Spectrometry 1988;16(1–12):99–111. doi:10.1002/bms.1200160119
9. Geiger T, Clarke S. Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides. Succinimide-linked reactions that contribute to protein degradation. Journal of Biological Chemistry 1987;262(2):785–794. doi:10.1016/S0021-9258(19)75855-4
10. Manning MC, Chou DK, Murphy BM, Payne RW, Katayama DS. Stability of protein pharmaceuticals: an update. Pharmaceutical Research 2010;27(4):544–575. doi:10.1007/s11095-009-0045-6
11. D'Hondt M, Bracke N, Taevernier L, Gevaert B, Verbeke F, Wynendaele E, et al. Related impurities in peptide medicines. Journal of Pharmaceutical and Biomedical Analysis 2014;101:2–30. doi:10.1016/j.jpba.2014.06.012

Cosmic Peptides. (2026, October 25). Growth hormone–releasing hormone analogs. Cosmic Peptides Research Library. Retrieved October 26, 2026, from https://cosmicpeptides.com/research/peptides/families/ghrh

@misc{cosmicpeptides_research_peptides_families_ghrh,
  author       = {{Cosmic Peptides}},
  title        = {Growth hormone–releasing hormone analogs},
  howpublished = {Cosmic Peptides Research Library},
  year         = {2026},
  month        = oct,
  url          = {https://cosmicpeptides.com/research/peptides/families/ghrh},
  urldate      = {2026-10-26},
  note         = {Last reviewed 2026-10-25}
}

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