Everything below concerns Neurotrophic factor. We keep the language plain, cite what the science says, and separate well-supported claims from open questions.
Last reviewed on 2025-09-10. Where a claim depends on a specific study, the study is described rather than over-claimed.
Development work on the compound began in the 1980s and 1990s at the Institute of Molecular Genetics in Moscow, within the same research programme that produced the peptide Semax. Early investigators sought a tuftsin derivative with improved resistance to enzymatic breakdown and with activity in the central nervous system after peripheral administration. Most of the primary literature from this period was published in Russian, a factor that still shapes how easily the findings can be checked by outside groups.
Naming for this compound is not fully standardised in English sources. The spelling Selanc appears in some transliterations, and catalogue entries may instead list the peptide sequence itself as the identifier. Reference material sometimes groups it with other short synthetic peptides studied for behavioural effects, which can create confusion when citations are compared. Distinguishing the exact sequence from related tuftsin analogues is therefore a practical first step when reviewing any dataset or specification sheet.
Selank is a synthetic heptapeptide with the sequence Thr-Lys-Pro-Arg-Pro-Gly-Pro, frequently abbreviated as TKPRPGP. It was designed as a structural analogue of tuftsin, a naturally occurring tetrapeptide released by enzymatic cleavage of the immunoglobulin heavy chain. The two additional proline residues at the C-terminal end extend the parent chain and change how the molecule behaves in solution. The free peptide has a calculated molecular mass of approximately 751.9 g/mol and is generally supplied as a lyophilised white to off-white powder.
Proposed mechanisms center on modulation of the GABA system, but no single molecular target has been confirmed. Rodent studies report changes in GABA-A receptor expression and in the turnover of serotonin, dopamine, and norepinephrine in several brain regions. Increases in brain-derived neurotrophic factor and its receptor have also been described after repeated administration. These findings come largely from animal models, and the degree to which they describe human neurochemistry remains an open question. The mechanism is best characterized as multi-system and not fully resolved.
Pharmacokinetic data are limited. Like most short peptides, Selank is vulnerable to plasma and tissue peptidases, and its measured half-life in circulation is short, on a minutes scale. The Pro-Gly-Pro tail slows this degradation but does not eliminate it. Intranasal administration is the route described in most reports, with absorption through the nasal mucosa and a hypothesized path into the central nervous system that avoids the blood-brain barrier. Direct measurements of human brain exposure are unavailable, so distribution claims rest on inference from animal work.
| Property | Value | Notes |
|---|---|---|
| Chemical class | Synthetic heptapeptide | Tuftsin analogue |
| Sequence | Thr-Lys-Pro-Arg-Pro-Gly-Pro | Single-letter form: TKPRPGP |
| Molecular formula | C33H57N11O9 | Calculated for the free peptide |
| Molecular weight | About 751.9 g/mol | Derived from the sequence |
| Appearance | White to off-white powder | Typical lyophilised form |
Purity assessment relies mainly on reverse-phase high-performance liquid chromatography with ultraviolet detection. Because the peptide lacks a strong chromophore, detection often uses backbone absorbance near 214 nm. Identity is confirmed by mass spectrometry, typically electrospray ionization or matrix-assisted laser desorption, comparing the measured mass against the expected value. Amino acid analysis can verify composition after acid hydrolysis. Diastereomer content and residual counterions are reported less often, although both can influence biological assays.
Lyophilized material is generally stable for extended periods when kept dry at or below minus twenty degrees Celsius. Working solutions are less stable, and common practice is to aliquot and freeze them so that repeated freeze-thaw cycles are avoided. Aqueous solutions are sensitive to pH extremes and to microbial growth, so short-term storage at refrigerator temperature is typical. Oxidation and hydrolysis are the principal degradation routes. Reconstitution with sterile water or a mild buffer is standard, and solutions should be protected from light.
Regulatory treatment varies by jurisdiction. In Russia the compound is a registered prescription product, while in the European Union and the United States it is generally handled as a research chemical without a marketing authorization. Suppliers therefore operate outside pharmaceutical oversight, and buyers rely on supplier documentation for purity and identity claims. Chain of custody and third-party testing are the main verification tools. Analysts note that the absence of a pharmacopoeial monograph for research-grade material limits standardization across vendors.
The compound has a calculated molecular weight near 751.9 daltons and carries a net positive charge at physiological pH because of its arginine residue. It dissolves freely in water and in common aqueous buffers, and typically appears as a white or off-white lyophilized powder. The amide backbone makes the molecule susceptible to peptidases, which limits oral use and favors intranasal or parenteral routes. Nomenclature in the literature varies: the substance is also described by the sequence abbreviation TP-7 and by a Russian trade designation.
Regulatory status differs sharply by region. Selank holds a Russian marketing authorization, where it is supplied mainly as nasal drops, while authorities elsewhere have not approved it for medical use. Material sold internationally is therefore usually labeled as a research chemical rather than a medicine. Peer-reviewed publications come predominantly from Russian laboratories, and sample sizes are generally small. Whether the compound produces comparable effects under independent, well-controlled replication remains an open question that the broader literature has not settled.
Selank is a synthetic heptapeptide developed in Russia during the 1990s. Researchers at the Institute of Molecular Genetics of the Russian Academy of Sciences designed it as a stabilized analog of tuftsin, a naturally occurring immunomodulatory tetrapeptide. The compound has been studied primarily for its reported anxiolytic and nootropic effects. It remains largely unknown in Western pharmacology and is not approved as a medicine by major regulators such as the FDA or the EMA.
The primary structure of Selank is Thr-Lys-Pro-Arg-Pro-Gly-Pro, corresponding to the molecular formula C33H57N11O9 and a monoisotopic mass of roughly 751.9 daltons. The N-terminal threonine and the arginine residue in the fourth position are shared with tuftsin, which carries the sequence Thr-Lys-Pro-Arg. The three additional residues at the C-terminus, Pro-Gly-Pro, extend the chain and are associated with greater resistance to enzymatic degradation. This extension also separates Selank from the shorter parent peptide.
Naming conventions place Selank in the same research family as Semax, another Russian-developed peptide investigated for cognitive effects. The two compounds share a lineage but differ in sequence and in the biological systems proposed as their targets. Semax descends from ACTH fragments, whereas Selank descends from tuftsin. Publications sometimes identify Selank by its full peptide sequence or by laboratory codes rather than one uniform trade name. Because replication outside Russia is limited, reports on its properties are best read alongside the study design and the purity of the material tested.
Most published work on selank originates from a small number of research groups in the Russian Federation. A large share of that record appears in Russian-language journals, which limits access for readers who rely on English-indexed databases. Independent replication by laboratories outside the original research network is sparse in publicly available sources. This concentration of origin and language is a frequently noted feature when the compound is summarized in broader reviews of synthetic peptides.
Reported pharmacological effects center on reduced anxiety-like behavior in animal models and on measures of memory and learning. Proposed contributing mechanisms include modulation of GABAergic signaling, shifts in monoamine turnover, and changes in the activity of enzymes that degrade neuropeptides. Effects on the expression of genes linked to neuroplasticity have also been described. No single molecular target is widely accepted, and whether the behavioral findings arise from one pathway or several remains an open question.
Selank is a synthetic heptapeptide with the sequence Thr-Lys-Pro-Arg-Pro-Gly-Pro. It was designed as a stabilized analogue of tuftsin, a naturally occurring tetrapeptide fragment derived from the immunoglobulin heavy chain. The additional Pro-Gly-Pro segment at the carboxyl terminus is intended to slow enzymatic cleavage. The compound is usually described in the literature as a synthetic peptide with anxiolytic and cognitive-related activity, a label that reflects a research context rather than an approved therapeutic category.
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Sources: en.wikipedia.org
== Medical uses == Blood is normally sterile. The presence of bacteria in the blood is termed bacteremia, and the presence of fungi is called fungemia. Minor damage to the skin or mucous membranes, which can occur in situations like toothbrushing or defecation, can introduce bacteria into the bloodstream, but this bacteremia is normally transient and is rarely detected in cultures because the immune system and reticuloendothelial system quickly sequester and destroy the organisms. Bacteria can enter the blood from infections such as cellulitis, UTIs and pneumonia; and infections within the vascular system, such as bacterial endocarditis or infections associated with intravenous lines, may result in a constant bacteremia. Fungemia occurs most commonly in people with poorly functioning immune systems. If bacteria or fungi are not cleared from the bloodstream, they can spread to other organs and tissues, or evoke an immune response that leads to a systemic inflammatory condition called sepsis, which can be life-threatening. When sepsis is suspected, it is necessary to draw blood cultures to identify the causative agent and provide targeted antimicrobial therapy. People who are hospitalized and have a fever, a low body temperature, a high white blood cell count or a low count of granulocytes (a category of white blood cells) commonly have cultures drawn to detect a possible bloodstream infection.
== Biosynthesis == The production of bottromycin by S. bottropensis and S. scabies, as well as the production of a bottromycin analog termed bottromycin D, has been studied. It was independently confirmed in 2012 by multiple groups that bottromycin is produced as a ribosomal peptide natural product that it subsequently post-translationally modified. Before this, it was unclear whether bottromycin was produced by nonribosomal peptide synthetase machinery (NRPS). The presence of amino acids other than the 20 proteinogenic amino acids is often a feature of NRPS products because NRPS machinery can directly incorporate other amino acids, among other chemical building blocks. Ribosomal peptide synthesis, which is the same machinery that produces all proteins found in the cell, is limited to the 20 proteinogenic amino acids. However, bottromycin was found to be a highly modified ribosomal peptide by a combination of genome mining and gene deletion studies. In ribosomal peptide synthesis, the final product results from modifications to a linear peptide starting material translated by the ribosome from an mRNA transcript. In S. scabies the precursor peptide, termed BtmD, is a 44-amino acid peptide. The precursor peptide is termed BmbC in S. bottropensis. The amino acids forming the bottromycin core are residues 2-9 in BtmD: Gly-Pro-Val-Val-Val-Phe-Asp-Cys. In bottromycin D, the sequence is Gly-Pro-Ala-Val-Val-Phe-Asp-Cys, and the precursor peptide is termed BstA. BstA shares high sequence homology with BtmD in the follower peptide region.
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Sources: en.wikipedia.org
The sequence is Thr-Lys-Pro-Arg-Pro-Gly-Pro, commonly written as TKPRPGP. It shares the first four residues with tuftsin and carries three prolines in the chain. The proline-rich tail is the main structural feature that separates it from the parent tetrapeptide.
Selank is a synthetic analogue built on the tuftsin tetrapeptide Thr-Lys-Pro-Arg. Extra proline residues were added to the C-terminus during design work. That modification is intended to make the peptide less vulnerable to rapid enzymatic degradation.
Transliteration from Russian produces variant spellings such as Selanc. Many suppliers avoid the trade-style name entirely and list the peptide sequence. Comparing sequences rather than names is the reliable way to confirm two entries describe the same molecule.
Reports describe effects on GABA-A receptor expression, monoamine turnover, and neurotrophic factor levels. These are proposed mechanisms drawn mainly from animal models. No single molecular target has been established.