Angiotensins and kinins

Angiotensins and kinins are short peptides cut from larger precursor proteins by proteases. They are among the best-characterized peptides in analytical chemistry and common calibration standards for mass spectrometry. Angiotensin II is angiotensin I less its C-terminal dipeptide, and angiotensin III and angiotensin (1–7) are shorter fragments still; bradykinin comes from a separate precursor, kininogen, and kallidin is bradykinin with an extra N-terminal lysine.

Members compared

Calculated from each structure

Peptide	Residues	Formula	Monoisotopic mass (Da)	Charge, pH 7	pI	Termini
Angiotensin (1–7)	7	C41H62N12O11	898.4661	0.2	7.54	free amine; free acid
Angiotensin III	7	C46H66N12O9	930.5076	1.2	9.35	free amine; free acid
Angiotensin II	8	C50H71N13O12	1,045.5345	0.2	7.54	free amine; free acid
Bradykinin	9	C50H73N15O11	1,059.5614	2.0	12.50	free amine; free acid
Angiotensin I	10	C62H89N17O14	1,295.6775	0.5	7.71	free amine; free acid
Kallidin	10	C56H85N17O12	1,187.6564	3.0	12.52	free amine; free acid

Sequences and relationships

Each member's sequence in three-letter code, and how it relates to Angiotensin I, worked out position by position from the structures. Members with no entry in the last column are not direct sequence relatives of Angiotensin I.

Relationship to Angiotensin I

Peptide	Sequence	Relationship
Angiotensin (1–7)	H-Asp-Arg-Val-Tyr-Ile-His-Pro-OH	Residues 1–7 of Angiotensin I
Angiotensin III	H-Arg-Val-Tyr-Ile-His-Pro-Phe-OH	Residues 2–8 of Angiotensin I
Angiotensin II	H-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-OH	Residues 1–8 of Angiotensin I
Bradykinin	H-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg-OH	—
Angiotensin I	H-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-OH	Reference sequence
Kallidin	H-Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg-OH	—

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

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

• Angiotensin II and Angiotensin III compared
• Kallidin and Bradykinin compared
• Angiotensin I and Angiotensin II 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). Angiotensins and kinins. Cosmic Peptides Research Library. Retrieved October 26, 2026, from https://cosmicpeptides.com/research/peptides/families/angiotensin-kinin

@misc{cosmicpeptides_research_peptides_families_angiotensin_kinin,
  author       = {{Cosmic Peptides}},
  title        = {Angiotensins and kinins},
  howpublished = {Cosmic Peptides Research Library},
  year         = {2026},
  month        = oct,
  url          = {https://cosmicpeptides.com/research/peptides/families/angiotensin-kinin},
  urldate      = {2026-10-26},
  note         = {Last reviewed 2026-10-25}
}

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