Tuftsin studies and research data
PepBank has no study results for Tuftsin yet. Data as of 2026-10-30.
Searches 0 results and 0 papers. Newer studies from Europe PMC
Tuftsin identity
Identifiers, parent molecule, targets and development stage, from curated data.
Tuftsin is the tetrapeptide H-Thr-Lys-Pro-Arg-OH, located at residues 289-292 of the IgG heavy chain CH2 domain and described in 1970 as a natural phagocytosis-stimulating peptide. Later studies report that it binds neuropilin-1 and, in microglia, signals through the TGF-beta pathway. It is the parent sequence of Selank.
- Kind
- Natural fragment · 4 residues
- Identifiers
- UniProtP01857 (opens in a new tab)ChEMBLCHEMBL4563222 (opens in a new tab)PubChem CID156080 (opens in a new tab)UNIIQF5336J16C (opens in a new tab)CAS9063-57-4PDB2ORZ (opens in a new tab)
- Parent
- Fragment of Immunoglobulin heavy constant gamma 1 (IgG1 heavy chain constant region) · residues 172-175Naim et al. 1989 (PMID 2475442): 'Tuftsin is located in the FC region of IgG between the 289 and 292 amino acid sequence of the CH2 domain.' Lukas et al. 1981 (PMID 7299136) studied peptides containing residues 289-292 or 282-292 of the second constant domain of human IgG1; its abstract does not use the word tuftsin. UniProt position 172-175 is an exact match of TKPR in P01857 (the only occurrence); EU numbering 289-292 minus the 117-residue offset of the UniProt entry gives 172-175.
- Development
- No known clinical developmentNo studies on ClinicalTrials.gov (queries with and without synonym expansion and a free-text search, 2026-10-09). ChEMBL gives no phase. Discovered by Najjar and Nishioka 1970 (PMID 4097539). Source (opens in a new tab)
Targets
| Target | Action | Evidence |
|---|---|---|
| Neuropilin-1NRP1O14786 (opens in a new tab) | Binds (ligand) | primary literatureSource (opens in a new tab) |
Sequence and structure
Residues, differences from the parent, calculated properties and 3D structure. Source values and calculated values are shown separately.
Sequence
4 amino acids
Parent: Immunoglobulin heavy constant gamma 1 (IgG1 heavy chain constant region)
No sequence is listed for the parent, so no alignment is shown.Naim et al. 1989 (PMID 2475442): 'Tuftsin is located in the FC region of IgG between the 289 and 292 amino acid sequence of the CH2 domain.' Lukas et al. 1981 (PMID 7299136) studied peptides containing residues 289-292 or 282-292 of the second constant domain of human IgG1; its abstract does not use the word tuftsin. UniProt position 172-175 is an exact match of TKPR in P01857 (the only occurrence); EU numbering 289-292 minus the 117-residue offset of the UniProt entry gives 172-175.
Properties
From identity sources
- Formula
- C21H40N8O6
- Molecular weight
- 500.6 g/mol
- Monoisotopic mass
- 500.3071 Da
- GSRS UNII QF5336J16C(opens in a new tab)retrieved 2026-10-08
- PubChem CID 156080(opens in a new tab)retrieved 2026-10-08
- ChEMBL CHEMBL4563222(opens in a new tab)retrieved 2026-10-08
- UniProt P01857(opens in a new tab)retrieved 2026-10-08
Calculated from the sequence
- Average mass
- 500.60 Da
- Sum of ExPASy residue masses + water · ExPASy Compute pI/Mw; FindMod
- Monoisotopic mass
- 500.3071 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)
- −2.675
- 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
- −30.20
- 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
- 5.76 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
Henderson-Hasselbalch, EMBOSS pKa set. Calculated, not measured.
Show as table
| pH | Net charge |
|---|---|
| 0 | 3.00 |
| 1 | 3.00 |
| 2 | 2.98 |
| 3 | 2.80 |
| 4 | 2.28 |
| 5 | 2.04 |
| 6 | 2.00 |
| 7 | 1.98 |
| 8 | 1.80 |
| 9 | 1.27 |
| 10 | 0.90 |
| 11 | 0.36 |
| 12 | −0.18 |
| 13 | −0.75 |
| 14 | −0.97 |
Composition
- Positive50% (2)K R
- Polar25% (1)T
- Special25% (1)P
4 residues. Each residue counts in one class; F and W count as aromatic.
3D structure
Loads the 3D viewer (3Dmol.js, about 150 KB) and the model file from RCSB PDB.
2D structure
Draws the structure in your browser with RDKit (about 2.3 MB, loaded once).
SMILES fromPubChem CID 156080(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)O)N)OWhat the studies measured
People first in each area, then animals, then lab cells. Counts are exact and come from studies that gave the peptide.
Newer studies
PepBank reads each paper before it shows the results. This search looks in Europe PMC for newer papers that PepBank has not read yet.
Tuftsin studies: 0 papers with results
No paper with results is linked to this peptide.