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Selank / Studies
Synthetic analog · 7 amino acids · 751.9 Da

Selank studies and research data

PepBank has 60 Selank studies with results. 58 of them gave Selank, with 221 results, grouped by what the studies measured. In each group, results from studies in people come first. Data as of 2026-10-30.

Searches 221 results and 73 papers. Newer studies from Europe PMC

Results in people
19
9% of 221 results
Results in animals
174
79% of 221 results
Results in lab cells
28
13% of 221 results
From computer models
0
0% of 221 results
The molecule

Selank identity

Identifiers, parent molecule, targets and development stage, from curated data.

Selank is the synthetic heptapeptide H-Thr-Lys-Pro-Arg-Pro-Gly-Pro-OH: the tuftsin sequence Thr-Lys-Pro-Arg followed by Pro-Gly-Pro. The Russian product information describes it as a synthetic analog of tuftsin with anxiolytic action; no molecular target is established. One radioligand study in rat brain membranes reports positive allosteric modulation of [3H]GABA binding (PMID 30255741); this is a hypothesis, not an established target. It is registered in Russia as 0.15% nasal drops (holder Peptogen) and has no FDA or EMA approval.

Kind
Synthetic analog · 7 residues
Identifiers
PubChem CID11765600 (opens in a new tab)UNIITS9JR8EP1G (opens in a new tab)CAS129954-34-3
Parent
Analog of TuftsinRussian product information (Vidal): 'synthetic analog of the endogenous peptide tuftsin'. Sequence comparison: Selank TKPRPGP (GSRS) begins with tuftsin TKPR (GSRS QF5336J16C).
Development
Approved in Russia only (registered as Селанк)Peptogen Innovative Research and Production Center, JSC (registration holder in Russia, per Vidal)Registered in Russia (Vidal listing). No FDA or EMA approval. Registrations in other countries were not checked. No studies on ClinicalTrials.gov when synonym expansion is off (2026-10-09); with expansion, 'Selank' returns 2 unrelated brain-stimulation studies. Source (opens in a new tab)

Targets

No molecular target is recorded for this peptide.

Sequence and structure

Residues, differences from the parent, calculated properties and 3D structure. Source values and calculated values are shown separately.

Sequence

7 amino acids

H-
Residues 1 to 7:
TKPRPGP
-OH
  • PositiveK R H
  • PolarS T N Q
  • SpecialC G P

Alignment to Tuftsin

Calculated from the two sequences. Curated notes are shown as given.

4 of 4 aligned residues identical (100%) · 3 added residues · Tuftsin 1–4

  • Top row: Tuftsin (parent)
  • Bottom row: Selank
TKPR
  • Same as parent
  • Substituted
  • Non-canonical or D-form
  • Added
  • Gap
  • Modified side chain or end

Differences from the parent

  1. 1Not in parent · analog 5+ Pro · Added residue
  2. 2Not in parent · analog 6+ Gly · Added residue
  3. 3Not in parent · analog 7+ Pro · Added residue

Basis: Russian product information (Vidal): 'synthetic analog of the endogenous peptide tuftsin'. Sequence comparison: Selank TKPRPGP (GSRS) begins with tuftsin TKPR (GSRS QF5336J16C).

Calculated from the two sequences with @pepdb/chem alignToParent (ungapped unless a gap scores higher). The record’s curated notes are shown as given.

Properties

From identity sources

Formula
C33H57N11O9
Molecular weight
751.9 g/mol
Monoisotopic mass
751.4341 Da

Calculated from the sequence

Average mass
751.88 Da
Sum of ExPASy residue masses + water · ExPASy Compute pI/Mw; FindMod
Monoisotopic mass
751.4341 Da
Sum of ExPASy residue masses + water · ExPASy FindMod
Isoelectric point (pI)
11.65
pH of zero net charge, EMBOSS pKa set · EMBOSS iep, Epk.dat
Net charge at pH 7.4
1.94
Henderson-Hasselbalch, EMBOSS pKa set · EMBOSS iep, Epk.dat
GRAVY (hydropathy)
−2.043
Mean Kyte-Doolittle hydropathy · Kyte and Doolittle 1982
Negative: hydrophilic on average.
Extinction coefficient, 280 nm (Cys reduced)
0 M⁻¹ cm⁻¹
5500 x Trp + 1490 x Tyr · Pace et al. 1995 (ExPASy ProtParam)
No Trp or Tyr: absorbance at 280 nm cannot measure this peptide.
Instability index
14.54
Dipeptide instability weights (DIWV) · Guruprasad et al. 1990
40 or below: classed as stable (ExPASy).
Aliphatic index
0.0
Mole % A + 2.9 V + 3.9 (I + L) · Ikai 1980
Boman index
3.16 kcal/mol
Mean solubility value (negated) · Boman 2003
Above 2.48: high protein-binding potential (Boman).
Hydrophobic moment (μH)
Not calculated
The sequence is too short for this method.
pI with each pKa set
EMBOSS 11.65Bjellqvist (ExPASy) 11.00IPC peptide 11.54IPC protein 10.61
  • Defined and validated for proteins; use with care for short peptides.
  • Assumes an ideal alpha helix. Many short peptides are not helical.

@pepdb/chem 0.2.0 · EMBOSS pKa set · ExPASy residue masses

Net charge by pH

pI 11.65 · Net charge at pH 7.4: 1.94

Point or use arrow keys

Net charge of Selank from pH 0 to 14 (EMBOSS pKa set). Isoelectric point 11.65. Net charge at pH 7.4: 1.94.−10+1+2+302468101214pHNet chargepH 7.4pI 11.65

Henderson-Hasselbalch, EMBOSS pKa set. Calculated, not measured.

Show as table
pHNet charge
03.00
13.00
22.98
32.80
42.28
52.04
62.00
71.98
81.80
91.27
100.90
110.36
12−0.18
13−0.75
14−0.97

Composition

  • Positive29% (2)
  • Polar14% (1)
  • Special57% (4)

7 residues. Each residue counts in one class; F and W count as aromatic.

A Ala0 · 0%
I Ile0 · 0%
L Leu0 · 0%
M Met0 · 0%
V Val0 · 0%
F Phe0 · 0%
W Trp0 · 0%
Y Tyr0 · 0%
H His0 · 0%
K Lys1 · 14%
R Arg1 · 14%
D Asp0 · 0%
E Glu0 · 0%
N Asn0 · 0%
Q Gln0 · 0%
S Ser0 · 0%
T Thr1 · 14%
C Cys0 · 0%
G Gly1 · 14%
P Pro3 · 43%

3D structure

No 3D structure

No experimental structure (PDB) and no UniProt entry for an AlphaFold model are listed for this peptide. Synthetic peptides often have neither. The sequence view above is the reference.

2D structure

Draws the structure in your browser with RDKit (about 2.3 MB, loaded once).

SMILES fromPubChem CID 11765600(opens in a new tab)

C[C@H]([C@@H](C(=O)N[C@@H](CCCCN)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCCN=C(N)N)C(=O)N2CCC[C@H]2C(=O)NCC(=O)N3CCC[C@H]3C(=O)O)N)O
Results by area

What the studies measured

People first in each area, then animals, then lab cells. Counts are exact and come from studies that gave the peptide.

Trials and papers
Status and safety
Data

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