GHRP-6 and Hexarelin compared

Hexarelin is GHRP-6 with one added methyl group, on the indole ring of the D-tryptophan at position 2. Everything else is identical.

Sequences side by side

Aligned from residue 1: 5 positions identical, 1 substituted. In each column the upper residue is GHRP-6's and the lower is Hexarelin's. Substituted positions are highlighted.

Both have the same termini: free amine and amide.

Calculated properties

Calculated from each structure

Property	GHRP-6	Hexarelin	Difference (Hexarelin − GHRP-6)
Residues	6	6	0
Molecular formula	C46H56N12O6	C47H58N12O6
Monoisotopic mass (Da)	872.4446	886.4602	+14.0157
Average mass (g/mol)	873.03	887.06	+14.03
Net charge at pH 7	2.2	2.2	0.0
Isoelectric point	none	none
Hydropathy (GRAVY)	-0.72	not calculated
ε280 (M−1 cm−1)	11,000	not calculated

Telling them apart by mass spectrometry

The monoisotopic masses differ by 14.0157 Da, which any routine mass spectrometer resolves.

Expected protonated ions (monoisotopic m/z)

Ion	GHRP-6	Hexarelin
[M+H]+	873.4519	887.4675
[M+2H]2+	437.2296	444.2374

Telling them apart by HPLC

A hydropathy comparison is not calculated because one of them contains residues outside the standard scale. Retention depends on the whole molecule and on the method, so the order is confirmed by running both, or by mass spectrometry of each peak.

Analytical variants each can form

The sequence-specific variants from each entry. A variant only one of them can form is a quick way to tell which is which, and a reminder of what to look for in each.

Sequence-specific variants

Variant	Mass change	GHRP-6	Hexarelin
Tryptophan oxidation	+15.995 or +31.990 Da	Yes	Yes
Stereochemistry	0 Da	Yes	Yes
C-terminal amide	free-acid variant +0.984 Da	Yes	Yes

Full details, with isotope patterns and fragment ions, are on each entry: GHRP-6 and Hexarelin. Both are compared with the rest of their family on the family page.

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). GHRP-6 and Hexarelin compared. Cosmic Peptides Research Library. Retrieved October 26, 2026, from https://cosmicpeptides.com/research/peptides/compare/ghrp-6-vs-hexarelin

@misc{cosmicpeptides_research_peptides_compare_ghrp_6_vs_hexarelin,
  author       = {{Cosmic Peptides}},
  title        = {GHRP-6 and Hexarelin compared},
  howpublished = {Cosmic Peptides Research Library},
  year         = {2026},
  month        = oct,
  url          = {https://cosmicpeptides.com/research/peptides/compare/ghrp-6-vs-hexarelin},
  urldate      = {2026-10-26},
  note         = {Last reviewed 2026-10-25}
}

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