Selank

Key facts

01 What Is Selank?

This is a short synthetic peptide of seven amino acids. It was developed in Russia as an analogue of tuftsin ^[2], a four-residue peptide that occurs naturally as a fragment of immunoglobulin G ^[1]. The name refers to one defined sequence, so unlike some catalog names it doesn't hide competing definitions.

FDA's Global Substance Registration System records the substance under that name, with the synonyms TP-7 and Selanc, and links it to the same PubChem record used on this page. You'll find it in the literature mainly in Russian laboratory and animal studies, often alongside its sister peptide Semax.

Vinnix doesn't sell it as a standalone vial. It is one of two components in the Selank + Semax research blend, and this page is the reference entry for the compound itself.

02 Selank Sequence and Origin

Tuftsin, Thr-Lys-Pro-Arg, was first described in 1970 as a natural peptide that stimulates phagocytic cells ^[1]. It is also broken down quickly in biological fluids ^[2]. The newer peptide keeps those four residues and extends the C-terminus with Pro-Gly-Pro, giving the heptapeptide below.

The added Pro-Gly-Pro belongs to a family of proline-rich fragments that Russian groups call glyprolines. Ashmarin and colleagues described hybrid, or "chimeric", peptides that join a regulatory sequence to a glyproline tail, and this peptide is one of their examples ^[3]. Peptides rich in proline tend to resist some peptidases, which is the usual rationale given for the design ^[4].

Two basic residues, lysine and arginine, give the molecule a net positive charge near neutral pH. That matters in the lab: it affects retention on reversed-phase HPLC and makes the peptide pick up protons readily in electrospray mass spectrometry.

03 Molecular and Registry Data

The identity values below come from PubChem and FDA GSRS. They describe the free peptide; a supplied material may also contain counter-ions such as acetate, which change the weight of the powder but not the peptide itself (see what molecular weight means).

04 Published Research

The published literature is small and mostly preclinical. Much of it appears in Russian-language journals, and very little has been repeated by independent groups elsewhere. The studies below show the kinds of questions laboratories have asked.

• Gene expression. An animal study measured the expression of inflammation-related genes in mouse spleen after exposure to the peptide ^[5].
• Enzyme studies. An in vitro study compared how Selank and Semax affected enkephalin-degrading enzymes in human serum samples ^[6].
• Animal models. A rat study examined Selank and Semax in a 6-OHDA lesion model ^[7].
• Stability. Reviews of proline-containing peptides discuss how glyproline-tailed sequences break down in biological media ^[4].

None of this establishes safety or any effect in humans, and it is not an approved medicine in the United States. Our guide to in vitro and in vivo research explains why the study type matters when reading these papers.

05 Laboratory Identification

Identity is confirmed by mass spectrometry: the measured mass should match 751.43 Da for the neutral molecule, which appears near m/z 752.44 as the singly protonated ion. HPLC then reports purity as the main peak's share of total peak area. In a blend, each of the two peptides should appear as separate, labeled peaks, each with its own result, as described in peptide testing and analysis.

06 Vinnix Products That Contain Selank

Vinnix offers this compound only inside the Selank + Semax blend (SKU XS20, 20 mg total per vial). The amount of each peptide is reported on the batch record. Batch reports are listed in the COA Library as each batch is released, and the vial's batch number is what links the two.

REFScientific references

1. Najjar VA, Nishioka K. "Tuftsin": a natural phagocytosis stimulating peptide. Nature. 1970;228(5272):672-673. PubMed 4097539
   original research (peptide isolation)
2. Siebert A, Gensicka-Kowalewska M, Cholewinski G, Dzierzbicka K. Tuftsin - Properties and Analogs. Curr Med Chem. 2017;24(34):3711-3727. PubMed 28745220
   review
3. Ashmarin IP, Samonina GE, Lyapina LA, Kamenskii AA, et al. Natural and hybrid ("chimeric") stable regulatory glyproline peptides. Pathophysiology. 2005;11(4):179-185. PubMed 15837162
   review
4. Shevchenko KV, Nagaev IY, Andreeva LA, Shevchenko VP, Myasoedov NF. [Stability of proline-containing peptides in biological media]. Biomed Khim. 2019;65(3):180-201. PubMed 31258142
   review
5. Kolomin T, Shadrina M, Andreeva L, et al. Expression of inflammation-related genes in mouse spleen under tuftsin analog Selank. Regul Pept. 2011;170(1-3):18-23. PubMed 21609736
   animal study
6. Kost NV, Sokolov OIu, Gabaeva MV, et al. [Semax and selank inhibit the enkephalin-degrading enzymes from human serum]. Bioorg Khim. 2001;27(3):180-183. PubMed 11443939
   in vitro study
7. Slominsky PA, Shadrina MI, Kolomin TA, et al. Peptides semax and selank affect the behavior of rats with 6-OHDA induced PD-like parkinsonism. Dokl Biol Sci. 2017;474(1):106-109. PubMed 28702721
   animal study