AOD-9604

A 16-residue synthetic peptide: residues 177–191 of human growth hormone with an added N-terminal tyrosine, closed by one disulfide bond. Every value on this page is calculated from the structure shown, by the method and constants in the sources below; measured values for a particular lot are on its certificate of analysis.

Structure

Three-letter code: H-Tyr-Leu-Arg-Ile-Val-Gln-Cys-Arg-Ser-Val-Glu-Gly-Ser-Cys-Gly-Phe-OH

One-letter code: YLRIVQCRSV EGSCGF

• 16 residues
• N-terminus: free amine
• C-terminus: free acid
• 1 disulfide bond

Calculated properties

Calculated from the structure

Property	Value
Molecular formula	C78H123N23O23S2
CAS Registry Number	221231-10-3
Average molecular weight	1,815.10 g/mol
Monoisotopic mass	1,813.8604 Da
Net charge at pH 7	1.0
Isoelectric point	9.35
Molar absorption coefficient, 280 nm	1,615 M−1 cm−1
Hydropathy (GRAVY)	0.30

Net charge across the pH range

pH 2	pH 4	pH 6	pH 7	pH 8	pH 10	pH 12
3.0	1.8	1.0	1.0	0.8	-0.4	-1.5

Composition: Arg 2, Cys 2, Gly 2, Ser 2, Val 2, Gln 1, Glu 1, Ile 1, Leu 1, Phe 1, Tyr 1.

Expected mass spectrometry ions

The protonated ions expected in positive-mode electrospray, from the monoisotopic mass, and the common sodium and potassium adducts. MALDI spectra show mainly [M+H]⁺.

Expected ions (monoisotopic)

Ion	m/z
[M+H]+	1,814.8676
[M+2H]2+	907.9375
[M+3H]3+	605.6274
[M+Na]+	1,836.8496
[M+K]+	1,852.8235

Isotope pattern

Natural carbon-13, nitrogen-15, oxygen-18, sulfur-34 and deuterium spread each ion over a cluster of peaks about 1 Da apart (1/z on the m/z scale). The monoisotopic peak is the most abundant.

Isotope peaks (relative abundance, most abundant = 100)

Peak	Abundance	Neutral mass	[M+H]+	[M+2H]2+	[M+3H]3+
M (monoisotopic)	100.0	1,813.8604	1,814.8676	907.9375	605.6274
M+1	96.6	1,814.8632	1,815.8704	908.4389	605.9617
M+2	59.9	1,815.8644	1,816.8716	908.9395	606.2954
M+3	27.7	1,816.8655	1,817.8728	909.4400	606.6291
M+4	10.4	1,817.8665	1,818.8738	909.9405	606.9628
M+5	3.3	1,818.8676	1,819.8749	910.4411	607.2965
M+6	0.9	1,819.8688	1,820.8761	910.9417	607.6302

Fragment ions (MS/MS)

In tandem mass spectrometry, a peptide closed by a disulfide bond does not break into the simple b- and y-ion ladder: a single cleavage inside the ring leaves it in one piece, so ring fragments need two cleavages and are not listed here. Reducing the disulfides before analysis is the usual way to sequence such a peptide.

What to watch for analytically

Variants this sequence can give, from its chemistry. They are what an HPLC or mass spectrometry result for this peptide is read against; none is a statement about a particular lot. Where synthesis variants come from is explained in How synthetic peptides are made.

Sequence-specific variants

Variant	Mass change	Why
Glutamine deamidation	+0.984 Da	Glutamine at position 6 can also deamidate, much more slowly than asparagine.
Disulfide state	reduced form +2.016 Da	The disulfide bond can be reduced, and intermolecular disulfides give dimers at about twice the mass.
Synthesis-related variants	e.g. +252.082 Da (Pbf), minus a residue (deletion)	As for any synthetic peptide, deletion sequences and incompletely deprotected forms can occur; on arginine, a residual Pbf protecting group adds 252.082 Da.

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). AOD-9604: peptide reference entry. Cosmic Peptides Research Library. Retrieved October 26, 2026, from https://cosmicpeptides.com/research/peptides/aod-9604

@misc{cosmicpeptides_research_peptides_aod_9604,
  author       = {{Cosmic Peptides}},
  title        = {AOD-9604: peptide reference entry},
  howpublished = {Cosmic Peptides Research Library},
  year         = {2026},
  month        = oct,
  url          = {https://cosmicpeptides.com/research/peptides/aod-9604},
  urldate      = {2026-10-26},
  note         = {Last reviewed 2026-10-25}
}

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