If you have been reading about tuftsin and want a single page that covers the useful parts, this is it: definitions, context, how it is studied, and the questions that come up repeatedly.
Updated 2026-08-01. Numbers and descriptions here follow the published literature rather than marketing material.
Once dissolved, the peptide is markedly less stable than the dry powder. Aqueous solutions are subject to backbone hydrolysis and to microbial growth when they are handled without sterile technique. Buffered solutions near neutral pH are common for short-term laboratory work, while acidic conditions are sometimes used to improve solubility. Analytical laboratories generally prepare working solutions fresh rather than storing them, and a residual water film left in a reopened vial can seed degradation even when the container appears dry.
Reversed-phase high-performance liquid chromatography is the standard technique for estimating peptide purity. The result is a peak-area percentage, which describes how much of the detected material elutes as the main peak in one run. Mass spectrometry confirms the molecular mass and can reveal truncated, adducted, or otherwise modified species. Amino acid analysis or tandem mass spectrometry can address sequence fidelity when identity is in doubt. None of these measurements, taken alone, establishes that a sample is fit for any specific purpose.
Lyophilized selank is normally supplied as a dry powder and is considered stable for extended periods when kept cold and dry. Moisture uptake is the main practical threat, because absorbed water promotes both hydrolysis and aggregation in the solid state. Vials are usually warmed to room temperature before opening so that condensation does not form on the powder. Supplier documentation commonly specifies -20 °C for routine storage, with -80 °C used for material intended to be archived for years.
Identity and purity of selank are established with reversed-phase high-performance liquid chromatography coupled to mass spectrometry. The peptide elutes from C18 columns with acetonitrile gradients in water containing trifluoroacetic acid or formic acid, and detection is usually performed by ultraviolet absorbance near 214 nm. Electrospray ionization in positive mode gives a doubly protonated ion near m/z 377, consistent with a mass of about 752 Da. Amino acid analysis or tandem mass spectrometry of fragment ions confirms the sequence. Because the molecule has no aromatic residues, it lacks a usable 280 nm chromophore, so low-wavelength detection or mass spectrometry is required.
Peptide bonds in selank are susceptible to hydrolysis under strongly acidic or basic conditions, and the terminal proline residues are vulnerable to exopeptidase activity in biological samples. Lyophilized powder stored dry at -20 °C typically remains stable for extended periods, whereas aqueous solutions degrade faster and may lose measurable purity within days to weeks depending on pH, temperature, and microbial load. Repeated freeze-thaw cycles promote aggregation and adsorption to container surfaces. For analytical work, solutions are usually prepared fresh, kept cold, and used within a single working day.
Handling follows standard practice for research peptides. Material is weighed in a low-humidity environment because the powder absorbs atmospheric moisture. Purity is reported as the percentage area of the main peak in a chromatogram, with specifications commonly set at 95 percent or higher; values below that threshold indicate the presence of truncated or modified species. Residual trifluoroacetate from purification is often present and may affect mass balance. Certificates of analysis should state the analytical method, the column and gradient used, and the lot-specific retention time so that results can be compared across suppliers.
| Property | Value | Notes |
|---|---|---|
| Typical purity specification | 95 percent or higher by RP-HPLC | Area percentage of the main peak |
| Identity confirmation | Electrospray ionization mass spectrometry | Observed mass compared with the theoretical value near 751.9 Da |
| Recommended dry storage | -20 °C, desiccated | -80 °C for multi-year archival material |
| Solution handling | Prepare fresh; avoid long storage | Sterile filtration reduces microbial load |
| Common synonyms | TKPRPGP; TP-7 | Sequence code and laboratory designation used interchangeably |
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.
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.
Quantification in biological matrices relies on liquid chromatography coupled to tandem mass spectrometry with stable-isotope internal standards. Low plasma concentrations and adsorption to container surfaces both complicate measurement. Solid-phase extraction is often needed to reduce matrix interference before injection. Reported limits of quantification differ widely between laboratories, which makes direct comparison of pharmacokinetic results difficult and limits meta-analysis.
Peptide bonds are vulnerable to protease attack, and Selank is no exception. Measured half-life in serum is short, on the order of minutes in several reports, which explains why intranasal administration is the common route described in the literature. Absorption across the nasal mucosa partially bypasses first-pass hepatic metabolism. Quantitative data on human bioavailability remain limited and are difficult to compare across studies.
Lyophilised material kept dry at minus 20 degrees Celsius or colder is the most stable form, and suppliers commonly state a shelf life of two years or more under those conditions. Once dissolved, degradation accelerates through hydrolysis and deamidation, particularly at alkaline pH or elevated temperature. Working solutions are usually divided into single-use aliquots to avoid repeated freeze-thaw cycles. The choice of reconstitution solvent affects both stability and the ionic strength of the final preparation.
Experiments on its genotoxicity at high doses are inconsistent. Its oxidized form TBBQ may be responsible for some toxic effects. There exists a wide margin of safety between food-additive doses and doses used in studies. There have been reports of vision disturbances in individuals exposed to this chemical.
The Journal of Psychiatric Research is a monthly peer-reviewed medical journal covering research in four major areas of psychiatry: clinical studies on normal and pathological human behavior; basic studies in psychiatry and related fields; clinical laboratory techniques such as neuroimaging, spectroscopy and other computer techniques used in research; advances in research methodology, including the clinical use of recent research findings. The journal was established in 1961 and is published by Elsevier. The current editor-in-chief is Eric Hollander (Albert Einstein College of Medicine). According to the Journal Citation Reports, the journal has a 2015 impact factor of 4.465.
== Use == A common way to synthesize an NHS-activated acid is to mix NHS with the desired carboxylic acid and a small amount of an organic base in an anhydrous solvent. A coupling reagent such as dicyclohexylcarbodiimide (DCC) or 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC) is then added to form a highly reactive activated acid intermediate. NHS reacts to create a less labile activated acid. The group is usually written as SuO- or -OSu in chemical notation. Such an ester with acid and NHS, sometimes called succinate ester, is stable enough to be purified and stored at low temperatures in the absence of water and, as such, is commercially available. NHS esters are commonly used for protein modification (e.g. an NHS ester of fluorescein is commercially available, and can be added to a protein to obtain a fluorescently labeled protein in a straightforward reaction and purification step). NHS can be used with EDC to immobilize enzymes for biosensor applications.
Sources: en.wikipedia.org
== Pharmacokinetics == When comparing the pharmacokinetic properties of spironolactone and eplerenone, it is clear that the two drugs differ. Spironolactone has shorter half-life (t1/2 = 1.3-1.4 hours) than eplerenone (t1/2 = 4–6 hours). Eplerenone goes through rapid metabolism by the liver to inactive metabolites (t1/2 = 4–6 hours). However, spironolactone is metabolized to three active metabolites, which give it prolonged activity (13.8 – 16. 5 hours). Spironolactone has a long half-life and is excreted 47-51% through kidneys. Patients with chronic kidney disease therefore require close monitoring when taking the drug. Spironolactone is also eliminated through feces (35-41%). The excretion of eplerenone is 67% through kidneys and 32% through feces. The information about excretion plays a critical role when determining the appropriate doses for patients with renal and/or hepatic dysfunction. It is very important to adjust the doses for patients with renal dysfunction because if they fail to eliminate the drug through their kidneys it could accumulate in the body, causing high concentration of potassium in the blood.
=== Bee–Ber === Lorena S. Beese(20th–21st century). Biochemist at Duke University, known for structural biochemistry of DNA replication and protein prenylation enzymes. Member Natl. Acad. Sci. USA. Helmut Beinert (1913–2007). German born-American biochemist at the University of Wisconsin–Madison, a pioneer of and advocate for the use of electron paramagnetic resonance in biological systems. Member Natl. Acad. Sci. USA. Marlene Belfort (b. 1945). American biochemist at the New York State Department of Health involved in the discovery of self-splicing introns in bacteriophage. Member Natl. Acad. Sci. USA. Boris Pavlovich Belousov (1893–1970). Chemist and biophysicist in the Ministry of Health of the USSR who discovered the Belousov–Zhabotinsky reaction. Awarded the Lenin Prize (1980). Myron L. Bender (1924–1988). American biochemist at Northwestern University, who pioneered mechanistic studies of enzymes, especially chymotrypsin and other proteases. Member Natl. Acad. Sci. USA. Stephen J. Benkovic (b. 1938). American bioorganic chemist at Pennsylvania State University. Member Natl. Acad. Sci. USA. Steven A. Benner (b. 1954). American chemist at the University of Florida known for establishing synthetic biology and paleogenetics, aas wll as contributing to understanding of the origin of life; Paul Berg FRS (foreign member) (1926–2023). American biochemist at Stanford, known for pioneering work involving gene splicing of recombinant DNA. He was awarded the Nobel Prize in Chemistry in 1980. Helen M. Berman (b. 1943).
=== Light-distance === George Gamow discussed measurements of time such as the "light-mile" and "light-foot", the time taken for light to travel the specified unit distance, defined by "reversing the procedure" used in defining a light-year. A light-foot is roughly one nanosecond, and one light-mile is approximately five microseconds.
Hepatokines (Greek heapto-, liver; and -kinos, movement) are proteins produced by liver cells (hepatocytes) that are secreted into the circulation and function as hormones across the organism. Research is mostly focused on hepatokines that play a role in the regulation of metabolic diseases such as diabetes and fatty liver and include: Adropin, ANGPTL4, Fetuin-A, Fetuin-B, FGF-21, Hepassocin, LECT2, RBP4,Selenoprotein P, Sex hormone-binding globulin.
Sources: en.wikipedia.org
Sealed, desiccated storage at -20 °C or colder is the standard recommendation for research-grade material. Vials should reach room temperature before they are opened, which limits condensation. Repeated temperature cycling is discouraged.
A reported purity value reflects the share of the main peak in one chromatographic run and says nothing about identity. Confirming that the expected sequence is present requires a separate measurement such as mass spectrometry. Purity and identity are distinct questions.
A mass spectrum reports the molecular masses present in a sample and shows whether they match the value expected for selank, near 751.9 Da. It also flags common artifacts such as truncation or adduct formation. It does not establish correct stereochemistry or complete sequence order on its own.
Identity is confirmed by matching the retention time in reversed-phase chromatography against a reference standard and by measuring the molecular mass with mass spectrometry. Tandem mass spectrometry or amino acid analysis can verify the sequence of the seven residues. Because the peptide contains no aromatic amino acids, detection at 280 nm is not useful.