BPC-157

A linear, unmodified synthetic pentadecapeptide rich in proline, with free termini. 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-Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val-OH

One-letter code: GEPPPGKPAD DAGLV

• 15 residues
• N-terminus: free amine
• C-terminus: free acid

Calculated properties

Calculated from the structure

Property	Value
Molecular formula	C62H98N16O22
CAS Registry Number	137525-51-0
Average molecular weight	1,419.56 g/mol
Monoisotopic mass	1,418.7042 Da
Net charge at pH 7	-2.0
Isoelectric point	3.88
Molar absorption coefficient, 280 nm	No tryptophan, tyrosine or cystine: no absorbance at 280 nm; quantify at 205–220 nm instead.
Hydropathy (GRAVY)	-0.69

Net charge across the pH range

pH 2	pH 4	pH 6	pH 7	pH 8	pH 10	pH 12
1.9	-0.3	-2.0	-2.0	-2.2	-3.1	-3.9

Composition: Pro 4, Gly 3, Ala 2, Asp 2, Glu 1, Leu 1, Lys 1, Val 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]+	1,419.7114
[M+2H]2+	710.3594
[M+3H]3+	473.9087
[M+Na]+	1,441.6934
[M+K]+	1,457.6673

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	1,418.7042	1,419.7114	710.3594	473.9087
M+1	74.9	1,419.7071	1,420.7144	710.8608	474.2430
M+2	32.2	1,420.7098	1,421.7170	711.3622	474.5772
M+3	10.1	1,421.7124	1,422.7196	711.8635	474.9114
M+4	2.6	1,422.7149	1,423.7222	712.3647	475.2456
M+5	0.5	1,423.7174	1,424.7247	712.8660	475.5797

Fragment ions (MS/MS)

Collision-induced fragmentation breaks peptide bonds along the backbone. Fragments that keep the N-terminus are b ions; those that keep the C-terminus are y ions. Reading the ladder confirms the sequence residue by residue. Singly charged monoisotopic values, with doubly charged values beside them. The b ion containing every residue is rarely seen and the y ion containing every residue is the precursor itself, so neither is listed.

b and y ions

b#	b+	b2+	Residue	y+	y2+	y#
1	58.0287	29.5180	Gly	—	—	15
2	187.0713	94.0393	Glu	1,362.6900	681.8486	14
3	284.1241	142.5657	Pro	1,233.6474	617.3273	13
4	381.1769	191.0921	Pro	1,136.5946	568.8009	12
5	478.2296	239.6185	Pro	1,039.5419	520.2746	11
6	535.2511	268.1292	Gly	942.4891	471.7482	10
7	663.3461	332.1767	Lys	885.4676	443.2374	9
8	760.3988	380.7030	Pro	757.3727	379.1900	8
9	831.4359	416.2216	Ala	660.3199	330.6636	7
10	946.4629	473.7351	Asp	589.2828	295.1450	6
11	1,061.4898	531.2485	Asp	474.2558	237.6316	5
12	1,132.5269	566.7671	Ala	359.2289	180.1181	4
13	1,189.5484	595.2778	Gly	288.1918	144.5995	3
14	1,302.6325	651.8199	Leu	231.1703	116.0888	2
15	—	—	Val	118.0863	59.5468	1

Immonium ions (low-mass markers of the residues present): Gly 30.0338, Ala 44.0495, Pro 70.0651, Val 72.0808, Leu 86.0964, Asp 88.0393, Lys 101.1073, Glu 102.0550.

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
Synthesis-related variants	minus a residue (deletion)	As for any synthetic peptide, deletion sequences and incompletely deprotected forms can occur.

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). BPC-157: peptide reference entry. Cosmic Peptides Research Library. Retrieved October 26, 2026, from https://cosmicpeptides.com/research/peptides/bpc-157

@misc{cosmicpeptides_research_peptides_bpc_157,
  author       = {{Cosmic Peptides}},
  title        = {BPC-157: peptide reference entry},
  howpublished = {Cosmic Peptides Research Library},
  year         = {2026},
  month        = oct,
  url          = {https://cosmicpeptides.com/research/peptides/bpc-157},
  urldate      = {2026-10-26},
  note         = {Last reviewed 2026-10-25}
}

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PY  - 2026
DA  - 2026/10/25
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Y2  - 2026/10/26
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