Peptidase stability raises a handful of sensible questions. This page answers them in order, starting with the fundamentals and moving to applications.
This page was last updated on 2025-12-05 and is reviewed periodically as new material appears.
Development took place at the Institute of Molecular Genetics of the Russian Academy of Sciences, where a series of short peptides were designed in the 1980s and 1990s. Selank was selected from variants of tuftsin that showed resistance to plasma peptidases. Russian regulatory approval covers it as an anxiolytic agent given intranasally. Outside that market the compound is normally handled as a research chemical rather than a medicine, and no widely recognised international pharmacopoeial monograph exists. The name Selank is a coined trade designation rather than a systematic chemical name.
Enzymatic stability motivates the extra three residues at the carboxyl end. Native tuftsin is cleaved quickly by circulating aminopeptidases and carboxypeptidases, which limits its duration of action and its usefulness as a tool compound. Extending the chain with proline-rich segments is a common design tactic because proline constrains the backbone and slows proteolysis. The same Pro-Gly-Pro motif appears in other Russian-developed peptides of the era. Whether the full seven-residue chain is required for activity, or whether it acts mainly as a prodrug releasing tuftsin, remains unresolved.
Selank is a synthetic heptapeptide with the sequence Thr-Lys-Pro-Arg-Pro-Gly-Pro. Its four N-terminal residues reproduce tuftsin, a tetrapeptide fragment of the immunoglobulin heavy chain, while the C-terminal Pro-Gly-Pro extension is a synthetic addition. The peptide has a molecular mass near 752 daltons and carries a net positive charge at physiological pH because of the arginine and lysine side chains. Published indexes list it under the name Selank and the sequence abbreviation TKPRPGP. Solid-phase peptide synthesis is the standard production route for research quantities.
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.
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.
| Property | Value | Notes |
|---|---|---|
| Chemical class | Synthetic heptapeptide | Tuftsin analogue with a C-terminal Pro-Gly-Pro tail |
| Amino acid sequence | Thr-Lys-Pro-Arg-Pro-Gly-Pro | Abbreviated TKPRPGP in most catalogues |
| Molecular mass | About 752 Da | Value for the free peptide |
| Solubility | Freely soluble in water | Aqueous solutions are kept cold and used promptly |
| Typical storage | -20 °C, dry, protected from light | Applies to the lyophilised powder before reconstitution |
Quality assessment of Selank samples typically combines purity determination with identity confirmation and counter-ion analysis. Purity is usually reported as a percentage by chromatographic area, with values above 95 percent often quoted for research-grade material. Water content and residual solvents are checked in lyophilized batches because they affect both stability and accurate mass determination. A reported purity figure does not by itself establish that a sample is the intended sequence, so orthogonal methods are needed to rule out sequence isomers or truncation products.
Characterization of Selank in laboratory settings relies on standard peptide analytical techniques. Reverse-phase high-performance liquid chromatography separates the peptide from related impurities and degradation products, while mass spectrometry confirms molecular identity through accurate mass measurement. Amino acid analysis and peptide sequencing verify the primary structure when reference material is unavailable. Because Selank is a short chain, fragmentation-based analysis produces a diagnostic ion pattern that supports confident identification.
Published clinical evidence is limited. Most controlled trials were conducted in Russia, enrolled modest numbers of participants, and appeared in Russian-language journals, which restricts independent verification. Reported outcomes include lower anxiety scores, improved attention and memory measures, and changes in fatigue ratings. Reviews written in English note methodological limitations such as small samples and inconsistent endpoints. Whether the compound produces clinically meaningful benefit relative to established anxiolytics is therefore an open question rather than an established finding.
Selank is a synthetic heptapeptide with the sequence Thr-Lys-Pro-Arg-Pro-Gly-Pro. It was designed at the Institute of Molecular Genetics of the Russian Academy of Sciences as a structural analogue of tuftsin, a naturally occurring tetrapeptide fragment of the immunoglobulin heavy chain. The added Pro-Gly-Pro tail was intended to slow enzymatic degradation and extend biological activity. In Russia it is registered as an anxiolytic nasal preparation, while regulators elsewhere have not approved it for clinical use.
Proposed mechanisms centre on modulation of the GABAergic system, with reports of altered expression of genes related to GABA-A receptor subunits and changed monoamine turnover. Some studies describe inhibition of enkephalinase, the enzyme that degrades endogenous enkephalins, which may prolong opioid peptide signalling. Effects on brain-derived neurotrophic factor and on cytokine expression have also been reported. These findings come largely from animal models and small human studies, and the precise primary target remains unresolved.
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.
Clinical evidence comes mainly from small studies conducted in Russia, several of which were open-label or lacked robust blinding. Reported outcomes include lower anxiety scores, changes in attention measures, and effects on asthenic states following illness. Sample sizes are typically in the tens of participants, and independent replication outside the region is scarce. Reviews published in English generally note the limited methodological quality of the underlying trials. Whether the compound produces clinically meaningful effects under rigorous conditions remains unresolved.
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.
In 1912, Frederick Gowland Hopkins demonstrated that unknown accessory factors found in milk, other than carbohydrates, proteins, and fats were necessary for growth in rats. Hopkins received a Nobel Prize for this discovery in 1929. By 1913, one of these substances was independently discovered by Elmer McCollum and Marguerite Davis at the University of Wisconsin–Madison, and Lafayette Mendel and Thomas Burr Osborne at Yale University. McCollum and Davis ultimately received credit because they submitted their paper three weeks before Mendel and Osborne. Both papers appeared in the same issue of the Journal of Biological Chemistry in 1913. The "accessory factors" were termed "fat soluble" in 1918, and later "vitamin A" in 1920. In 1919, Harry Steenbock (University of Wisconsin–Madison) proposed a relationship between yellow plant pigments (β-carotene) and vitamin A. In 1931, Swiss chemist Paul Karrer described the chemical structure of vitamin A. Retinoic acid and retinol were first synthesized in 1946 and 1947 by two Dutch chemists, David Adriaan van Dorp and Jozef Ferdinand Arens.
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==== MeSH D06.472.334 – gonadal hormones ==== MeSH D06.472.334.500 – activins MeSH D06.472.334.500.500 – inhibin-beta subunits MeSH D06.472.334.734 – corpus luteum hormones MeSH D06.472.334.734.623 – progesterone MeSH D06.472.334.734.769 – relaxin MeSH D06.472.334.851 – gonadal steroid hormones MeSH D06.472.334.851.437 – estradiol congeners MeSH D06.472.334.851.437.249 – equilenin MeSH D06.472.334.851.437.374 – equilin MeSH D06.472.334.851.437.500 – estradiol MeSH D06.472.334.851.437.750 – estriol MeSH D06.472.334.851.437.750.320 – estetrol MeSH D06.472.334.851.437.968 – estrogenic steroids, alkylated MeSH D06.472.334.851.437.968.500 – ethinyl estradiol MeSH D06.472.334.851.437.968.500.250 – ethinyl estradiol-norgestrel combination MeSH D06.472.334.851.437.968.500.500 – mestranol MeSH D06.472.334.851.437.968.500.750 – quinestrol MeSH D06.472.334.851.437.984 – estrogens, catechol MeSH D06.472.334.851.437.984.350 – hydroxyestrones MeSH D06.472.334.851.437.988 – estrogens, conjugated (usp) MeSH D06.472.334.851.437.994 – estrogens, esterified (usp) MeSH D06.472.334.851.437.996 – estrone MeSH D06.472.334.851.687 – progesterone congeners MeSH D06.472.334.851.687.500 – pregnenolone MeSH D06.472.334.851.687.500.500 – 17-alpha-hydroxypregnenolone MeSH D06.472.334.851.687.750 – progesterone MeSH D06.472.334.851.687.750.074 – 20-alpha-dihydroprogesterone MeSH D06.472.334.851.687.750.099 – 5-alpha-dihydroprogesterone MeSH D06.472.334.851.687.750.478 – hydroxyprogesterones MeSH D06.472.334.851.687.750.478.400 – 17-alpha-hydroxyprogesterone MeSH D06.472.334.851.687.750.478.400.500 – pregnanetriol MeSH D06.472.334.851.687.750.739 – pregnanediol MeSH D06.472.334.851.968 – testosterone congeners MeSH D06.472.334.851.968.500 – androstane-3,17-diol MeSH D06.472.334.851.968.750 – androstenediol MeSH D06.472.334.851.968.875 – androstenedione MeSH D06.472.334.851.968.937 – androsterone MeSH D06.472.334.851.968.952 – dehydroepiandrosterone MeSH D06.472.334.851.968.952.300 – dehydroepiandrosterone sulfate MeSH D06.472.334.851.968.964 – dihydrotestosterone MeSH D06.472.334.851.968.968 – etiocholanolone MeSH D06.472.334.851.968.976 – nandrolone MeSH D06.472.334.851.968.984 – testosterone MeSH D06.472.334.851.968.984.500 – epitestosterone MeSH D06.472.334.851.968.984.750 – testosterone propionate MeSH D06.472.334.968 – inhibins MeSH D06.472.334.968.500 – inhibin-beta subunits MeSH D06.472.334.984 – testicular hormones
== Legality and Regulation == The Early Warning System (EWS), operated by the European Monitoring Centre for Drugs and Drug addiction (EMCDDA), overseas illicit substances that appear in the market. Established in 1997, It formed part of the framework that allows the European Union to rapidly detect NPS that pose a risk to the public's health. Due to the tightening of legislation, most NPS are now illegal in the UK and Germany. Upon the emergence of NPS, this agency responds in the following manner:
Protein phosphatase 1 subunits PP1β and PP1γ have been shown to form functional complexes with OGT. A synthetic phosphopeptide was able to be dephosphorylated and O-GlcNAcylated by an OGT immunoprecipitate. This complex has been referred to as a "yin-yang complex" as it replaces a phosphate modification with an O-GlcNAc modification. PP1γ also exists in a heterotrimer with OGT and URI under high glucose conditions. MYPT1 is another protein phosphatase subunit that forms complexes with OGT and is itself O-GlcNAcylated. MYPT1 appears to have a role in directing OGT towards specific substrates.
Sources: en.wikipedia.org
The explosive trace detectors utilizing AFPs, known as Fido Explosives Detectors, were originally developed under the Defense Advanced Research Projects Agency (DARPA) Dog’s Nose program and is now produced by FLIR Systems. The current generation, provides broad-band trace explosive detection and weighs less than 3 lbs. The sensitivity is in the order of femtogram (1 × 10−15 grams). This is the only such technology in the field that can achieve such sensitivity.
=== Form factor === The physical design of refrigerators also plays a large part in its energy efficiency. The most efficient is the chest-style freezer, as its top-opening design minimizes convection when opening the doors, reducing the amount of warm moist air entering the freezer. On the other hand, in-door ice dispensers cause more heat leakage, contributing to an increase in energy consumption.
Breakfast cereal is a category of food, including food products, made from processed cereal grains, that are eaten as part of breakfast or as a snack food, primarily in Western societies. Although warm, cooked cereals like oatmeal, maize, grits, and wheat farina have the longest history as traditional breakfast foods, branded and ready-to-eat cold cereals (many produced via the process of extrusion) appeared around the late 19th century. These processed, precooked, packaged cereals are most often served in a quick and simple preparation with dairy products, traditionally cow's milk. These modern cereals can also be paired with yoghurt or plant-based milks, or eaten plain. Fruit or nuts are sometimes added, and may enhance the nutritional benefits. Some companies promote their products for the health benefits that come from eating oat-based and high-fiber cereals. In the United States, cereals are often fortified with vitamins, but can still lack many of the vitamins needed for a healthful breakfast, and so initial marketing focused on making the new products "part of a complete breakfast". A significant proportion of packaged cereals have a high sugar content ("sugar cereals" or even "kids' cereals" in common parlance). These cereals are frequently marketed toward children (in television ads, comic books, etc.) and often feature a cartoon mascot and may contain a toy or prize.
The company was founded by Colonel Eli Lilly, a pharmaceutical chemist and Union army veteran of the American Civil War. Lilly served as the company president until his death in 1898. In 1869, after working for drugstores in Indiana, Lilly became a partner in a Paris, Illinois-based drugstore with James W. Binford. Four years later, in 1873, Lilly left the partnership with Binford, and returned to Indianapolis. In 1874, Lilly partnered with John F. Johnston, and opened a drug manufacturing operation called Johnston and Lilly. In 1876, Lilly dissolved the partnership, and used his share of the assets to open his own pharmaceutical manufacturing business, Eli Lilly and Company, in Indianapolis. The sign outside, above the shop's door, read: "Eli Lilly, Chemist." The Indiana Historical Society recreated a replica of the first Lilly laboratory on Pearl Street for its exhibition, "You Are There: Eli Lilly at the Beginning," at the Eugene and Marilyn Glick Indiana History Center in Indianapolis. The temporary exhibition (1 October 2016, to 20 January 2018) also included costumed interpreters portraying Colonel Lilly and others. In 1886, Ernest G. Eberhardt, a chemist, joined the company as its first full-time research scientist. Lilly began his manufacturing venture with three employees, including his son, Josiah (J. K.). One of the first medicines that Lilly produced was quinine, a drug used to treat malaria, a mosquito-borne disease. By the end of 1876, sales reached $4,470. Around 1890, Col.
=== Off-label drugs === Low-dose oral minoxidil Oral antiandrogens (androgen receptor antagonists) (e.g., spironolactone, cyproterone acetate, flutamide, bicalutamide) Oral estrogens (e.g., ethinylestradiol, estradiol) Topical antiandrogens (androgen receptor antagonists) (e.g., spironolactone, ketoconazole) Corticosteroids – alopecia areata (e.g., triamcinolone, clobetasol, fluocinonide, mometasone)
Sources: en.wikipedia.org
Selank is a seven-amino-acid peptide built from the tuftsin sequence plus a Pro-Gly-Pro tail. It is produced by chemical synthesis rather than extracted from a natural source. The free peptide is usually supplied as a lyophilised powder or in an aqueous formulation.
Tuftsin is a natural tetrapeptide derived from the Fc portion of immunoglobulin G. Selank retains that tetrapeptide at its N-terminus and adds three residues to improve resistance to enzymatic breakdown. The relationship is structural, and the two molecules are not interchangeable in experimental work.
It holds a product registration in Russia for intranasal use as an anxiolytic. Registrations of that kind are not automatically accepted by regulators elsewhere. In most other countries it is treated as an unapproved substance or a research material.
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.