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Compound monograph

Galanin (human 1-30)

Galanin is a thirty-residue human neuropeptide acting through the galanin receptor family, and the reference ligand against which spexin's receptor selectivity is measured.

Published: 2026-09-19Last updated: 2026-10-13Literature/identifier verification: 2026-09-17
Also known asGALGalanin(1-30)
Neuropeptides and derived fragments

01

Identity & nomenclature

Galanin is a thirty-residue human neuropeptide acting through the galanin receptor family, and the reference ligand against which spexin's receptor selectivity is measured.

Human galanin is thirty residues with a free acid terminus and is NOT interchangeable with the 29-residue amidated galanins from other species that appear throughout this literature as comparators; length, C-terminal sequence and terminal chemistry all differ. Galanin-like peptide is a different molecule, not an alias. PubChem CID 16133823 is retained for fully stereospecified human galanin(1–30) with free termini; CID 74765466 has the same connectivity but leaves stereochemistry undefined. And spexin is not a proteolytic fragment of galanin — the two are separate gene products that happen to share receptors.

Canonical name: Galanin.

Declared aliases and development codes: GAL, Galanin(1-30).

02

Molecular properties

Molecular formulaC139H210N42O43
Molecular mass3157.4 Da
CAS Registry Number119418-04-1
PubChem CID16133823
One-letter sequenceGWTLNSAGYLLGPHAVGNHRSFSDKNGLTS
Terminal groupsFree N-terminus; Free C-terminal carboxyl

Thirty residues with a FREE C-terminal carboxyl — not an amide. That distinguishes the human peptide from the 29-residue amidated galanins of several other species, which are widely used as comparators.

03

Structural characteristics

The cryo-EM study used galanin(1-30) and determined galanin-bound GALR1-Go and GALR2-Gq complexes, alongside a spexin-bound GALR2-Gq complex. The resolved galanin N-terminal region adopts a largely alpha-helical conformation in the extracellular vestibule, roughly parallel to the membrane. Its N-terminal residues 1-17 were well resolved; this does not establish structural detail for the entire human C-terminal segment. Functional measurements in the same study identified zinc as a negative allosteric regulator of GALR1 but not GALR2. The evolutionary comparison supplies family context; it does not establish a matched GALR3 potency comparison for this exact human thirty-residue free acid.

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

04

Molecular targets & mechanisms

Galanin receptors

GALR1 · GALR2 · GALR3 · GalR

The galanin receptor family comprises three G protein-coupled receptors. GALR1 and GALR3 signal through Gi/o, while GALR2 signals mainly through Gq/11. Spexin activates GALR2 and GALR3 but not GALR1 in the reported ligand panel. Structural studies compared galanin-bound GALR1-Go and GALR2-Gq with spexin-bound GALR2-Gq, providing evidence for ligand recognition and subtype-dependent coupling.

05

Analytical considerations

Establish the human C-terminal sequence and the free acid at serine 30 specifically; conserved N-terminal coverage is the region shared with other species' galanins and cannot identify the human peptide. Look explicitly for amidated contaminants and for species substitutions against sequence-defined standards. Similar receptor activation does not distinguish human galanin from other active galanin sequences, and a generic galanin immunoassay may resolve neither length nor terminal processing.

Disagreements and mix-ups

Points where sources disagree about this compound's identity, or where a name or form is easily confused with another, as noted in this record. The discrepancy register quotes the passage for each one.

What the studies reported

Each finding describes one cited study in its stated model. These observations are specific to that study and do not establish effects in other settings.

Cell and tissue studies

  • Human GALR1-Go and GALR2-Gq cryo-electron microscopy preparations

    Using human GALR1-Go and GALR2-Gq cryo-electron microscopy preparations, the study reported galanin-bound receptor complexes.

    Reference [1]

  • Human galanin-bound GALR1 and GALR2 structural preparations

    Using human galanin-bound GALR1 and GALR2 structural preparations, the study found a mainly alpha-helical peptide positioned in the extracellular vestibule nearly parallel to the membrane.

    Reference [1]

  • Human GALR1-expressing HEK-293T NanoBiT mini-G recruitment assay

    Using a human GALR1-expressing HEK-293T NanoBiT mini-G recruitment assay, the study measured zinc inhibition of galanin-associated receptor activation with an IC50 of 47.2 μM.

    Reference [1]

  • Human GALR2-expressing HEK-293T NanoBiT mini-G recruitment assay

    Using a human GALR2-expressing HEK-293T NanoBiT mini-G recruitment assay, the study observed little effect of zinc on galanin-induced receptor activation below millimolar zinc concentrations.

    Reference [1]

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.

A paper can report more than one kind of work. Each count opens those papers in the bibliography. Compare every record on the Evidence Map.

  1. Reference 1

    Structural insights into galanin receptor signaling.

    Jiang W, Zheng S

    Proceedings of the National Academy of Sciences of the United States of America · 2022-05-20 · Journal Article

    current
    PMID 35594396PMC9173784DOI 10.1073/pnas.2121465119SpexinGalanin (human 1-30)GALR1

  2. Reference 2

    Coevolution of the spexin/galanin/kisspeptin family: Spexin activates galanin receptor type II and III.

    Kim DK, Yun S, Son GH, Hwang JI, Park CR, Kim JI, Kim K, Vaudry H, Seong JY

    Endocrinology · 2014-02-11 · Journal Article

    current
    PMID 24517231DOI 10.1210/en.2013-2106SpexinKisspeptin-14Galanin (human 1-30)GALR1

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
Jiang W et al. 2022Study models reported: in vitro · from the abstract
Kim DK et al. 2014Study models reported: in vitro · from the abstract

Record history

Published 2026-09-19.

  • : Identity and nomenclature

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. Galanin (human 1-30). Published 2026-09-19; updated 2026-10-13. https://purelypeptides.org/research/compounds/galanin/

10

Methodology & citation verification

Reference identity is checked against official PubMed metadata. Local deterministic receipts bind each normalized title and canonical metadata record to its verification date. Scientific values remain absent when an authoritative source has not been verified.

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