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Compound monograph

Salmon calcitonin

Salmon calcitonin is a 32-residue peptide with a free N terminus, C-terminal prolinamide and a Cys1-Cys7 disulfide. This record describes the parent without counterion or hydration components.

Published: 2026-10-20Literature/identifier verification: 2026-10-20
Also known asCalcitonin salmon

01

Identity & nomenclature

Salmon calcitonin is a 32-residue peptide with a free N terminus, C-terminal prolinamide and a Cys1-Cys7 disulfide. This record describes the parent without counterion or hydration components.

Calcitonin salmon is an admitted word-order alias. This record identifies the full-length parent peptide; production method alone does not establish a distinct molecular species or universal equivalence between preparations. No unique PubChem CID is admitted because competing issuer records remain unresolved.

Declared aliases and development codes: Calcitonin salmon.

02

Molecular properties

Molecular formulaC145H240N44O48S2
Molecular mass3431.895 Da
CAS Registry Number47931-85-1
UNII7SFC6U2VI5
One-letter sequenceCSNLSTCVLGKLSQELHKLQTYPRTNTGSGTP
Three-letter sequenceCys–Ser–Asn–Leu–Ser–Thr–Cys–Val–Leu–Gly–Lys–Leu–Ser–Gln–Glu–Leu–His–Lys–Leu–Gln–Thr–Tyr–Pro–Arg–Thr–Asn–Thr–Gly–Ser–Gly–Thr–Pro
Terminal groupsFree N-terminus; C-terminal amidation

Positions count the 32-residue mature chain. All chiral residues are L; glycine is achiral. Val8, Lys11 and Pro32 are retained explicitly. Terminal amidation and the Cys1-Cys7 disulfide are recorded separately.

03

Structural characteristics

The 32-residue backbone has a free N terminus at Cys1 and a C-terminal amide at Pro32. Meyer et al. and the Japanese Pharmacopoeia XVIII connectivity diagram support the Cys1-Cys7 disulfide. Niall et al. provide sequence and terminal characterization; their tentative disulfide discussion is not used as the sole connectivity proof. Counterions, hydration components, synthetic intermediates and sulfur-modified derivatives are excluded from this parent.

  • Cys1-Cys7 intramolecular disulfide

Ring closures: covalent bonds between residues, by position counted from the first residue of the chain.

  • Disulfide Cys1–Cys7: thiol sulfur (Sγ) to thiol sulfur (Sγ). Source: PMID 2043752.

Terminal features: Free N-terminus, C-terminal amidation.

04

Molecular targets & mechanisms

05

Analytical considerations

The formula and 3431.895 Da average mass are calculated using CIAAW 2024 abridged atomic weights. Japanese Pharmacopoeia XVIII reports 3431.85, a non-defining difference of 0.045 Da (13.1125 ppm). PubChem reports 3431.9 under an average-mass convention; DailyMed prints 3432 without an established convention in the inspected description. Neither replaces the defined calculation. Niall et al. sequence determination and Meyer et al. synthetic-peptide NMR provide complementary identity evidence; a preparation-independent solution conformation is not assigned.

What the studies reported

No verified findings are published for this record under Content Policy v1.

06

Verified bibliography

Cited studies by type

The 2 papers this record cites, counted by the kind of work each reports. A count is the size of this record's selection, not of the research that exists, and says nothing about results, safety, effectiveness or approval.

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  1. Reference 1

    Amino acid sequence of salmon ultimobranchial calcitonin.

    Niall HD, Keutmann HT, Copp DH, Potts JT Jr

    Proceedings of the National Academy of Sciences of the United States of America · 1969-10 · Journal Article

    current
  2. Reference 2

    Solution structure of salmon calcitonin.

    Meyer JP, Pelton JT, Hoflack J, Saudek V

    Biopolymers · 1991-02-05 · Journal Article

    current

Study models of these references

What kind of experiment each cited paper reports, taken from its abstract unless marked. Not a summary of results.

ReferenceStudy models
Niall HD et al. 1969Chemical, structural or analytical study; no biological model reported
Meyer JP et al. 1991Chemical, structural or analytical study; no biological model reported

Record history

Published 2026-10-20.

No changes to this record's content have been recorded since publication.

Each entry names the parts of this record that changed on that date. Changes to links between records and to catalogue links are not listed. This history covers the tracked record fields; study findings are not listed here.

Cite this record: Purely Peptides Research Library. Salmon calcitonin. Published 2026-10-20. https://purelypeptides.org/research/compounds/salmon-calcitonin/

10

Methodology & citation verification

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