Compound monograph
Spadin
Spadin is a sortilin-propeptide-derived peptide reported to interact with sortilin and to inhibit the TREK-1 potassium channel, and the parent design from which PE 22-28 was derived.
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Identity & nomenclature
Spadin is a sortilin-propeptide-derived peptide reported to interact with sortilin and to inhibit the TREK-1 potassium channel, and the parent design from which PE 22-28 was derived.
Spadin derives from the propeptide released during sortilin maturation. Sortilin is also called neurotensin receptor 3. This entry specifies the eighteen-residue Tyr-extended form; the unqualified name spadin and the label PE(12-28) do not resolve the seventeen-versus-eighteen-residue distinction. The founding study describes a Tyr0 radioiodination site. Its labeled binding probe is a separate reagent, and an assay described only as spadin does not establish that every experiment used the same terminal form. PE 22-28 is a seven-residue designed truncation of the same propeptide sequence.
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Molecular properties
| Molecular formula | C96H142N26O22 |
|---|---|
| Molecular mass | 2012.3 Da |
| CAS Registry Number | 1270083-24-3 |
| PubChem CID | 91826106 |
| One-letter sequence | YAPLPRWSGPIGVSWGLR |
| Terminal groups | Free N-terminus; Free C-terminal carboxyl |
Eighteen residues with free termini. This record specifies the Tyr-extended form YAPLPRWSGPIGVSWGLR. The seventeen-residue sortilin-propeptide segment PE(12-28) is APLPRWSGPIGVSWGLR; the added tyrosine changes the residue composition by 163.06 Da.
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Structural characteristics
The founding study reported reciprocal immunoprecipitation of sortilin and TREK-1 and colocalization in cortical neurons. Binding assays reported approximately 10 nM affinity, and electrophysiology measured inhibition of TREK-1 activity in transfected cells, cultured hippocampal neurons and brain slices. A later study designed PE 22-28 from blood degradation products and measured TREK-1 inhibition in hTREK-1/HEK cells at approximately 0.1 nM, against 40-60 nM for the spadin comparator. That source is internally inconsistent about which peptide carries which value: its abstract and results report 0.12 nM for PE 22-28 and 0.10 nM for the Gly22-Ala analog, while its figure legend and discussion transpose the two. No single figure is reproduced here as though the source agreed with itself. These results establish the experimental design relationship; they do not establish endogenous production of the seven-residue peptide. The Tyr extension and radioiodination state must be tracked when comparing reagents.
Terminal features: Free N-terminus, Free C-terminal carboxyl.
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Molecular targets & mechanisms
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Analytical considerations
The first question for any sample is whether it begins Tyr-Ala or Ala: the tyrosine residue adds 163.06 Da monoisotopic, 163.18 Da average, and N-terminal fragmentation localises it. State which convention a reported figure uses; the recorded mass on this entry is an average mass. Radioiodinated Tyr-containing binding probes used in this literature are separate reagents and are not chemically identical to unlabelled spadin. For PE 22-28, verify the exact seven residues and the free acid, and exclude the Gly22-Ala analog and the biotinylated derivatives used in the same experiments — a shared TREK-1 response does not distinguish them.
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.
Often mixed up · Name or substance
Spadin: seventeen or eighteen residues
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
TREK-1-transfected COS-7 membrane homogenate radioligand competition assay
Using TREK-1-transfected COS-7 membrane homogenates in radioligand competition assays, the study reported spadin affinity of about 10 nM.
Reference [1]TREK-1-expressing COS-7 electrophysiology assay
Using a TREK-1-expressing COS-7 electrophysiology assay, the study observed blockade of channel activity with spadin.
Reference [1]Wild-type and kcnk2-null mouse CA3 hippocampal neurons in brain slices
In wild-type and kcnk2-null mouse CA3 hippocampal neurons in brain slices, the study observed TREK-1 blockade with spadin in wild-type tissue and no corresponding blockade in null tissue.
Reference [1]
Animal studies
Mice in five behavioral tests predicting an antidepressant response
In mice assessed with five behavioral tests predicting an antidepressant response, the study reported a depression-resistant phenotype with spadin.
Reference [1]
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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.
Reference 1
Spadin, a sortilin-derived peptide, targeting rodent TREK-1 channels: a new concept in the antidepressant drug design.Mazella J, Pétrault O, Lucas G, Deval E, Béraud-Dufour S, Gandin C, El-Yacoubi M, Widmann C, Guyon A, Chevet E, Taouji S, Conductier G, Corinus A, Coppola T, Gobbi G, Nahon JL, Heurteaux C, Borsotto M
PLoS biology · 2010-04-13 · Journal Article
currentReference 2
Shortened Spadin Analogs Display Better TREK-1 Inhibition, In Vivo Stability and Antidepressant Activity.Djillani A, Pietri M, Moreno S, Heurteaux C, Mazella J, Borsotto M
Frontiers in pharmacology · 2017-09-12 · 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.
| Reference | Study models |
|---|---|
| Mazella J et al. 2010 | Study models reported: in vitro; animal (mouse) · from the abstract |
| Djillani A et al. 2017 | Study models reported: in vitro; animal (mouse) · from the abstract |
Record history
Published 2026-09-19.
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. Spadin. Published 2026-09-19. https://purelypeptides.org/research/compounds/spadin/
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Methodology & citation verification
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