If you have been reading about TP-7 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.
Last reviewed on 2026-02-11. Where a claim depends on a specific study, the study is described rather than over-claimed.
Selank is a synthetic heptapeptide developed in Russia as a structural analogue of tuftsin, a naturally occurring immunomodulatory tetrapeptide. Its sequence, Thr-Lys-Pro-Arg-Pro-Gly-Pro, keeps the tuftsin core at the N-terminus and appends a Pro-Gly-Pro tail. Researchers at the Institute of Molecular Genetics in Moscow synthesized the compound during the 1990s while searching for peptides with combined anxiolytic and immunomodulatory activity. The added tail was intended to resist enzymatic cleavage and prolong the molecule's presence in circulation.
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.
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.
Peptide stability depends strongly on temperature, moisture, and pH. Lyophilized Selank is generally most stable when stored cold and dry, with freezer temperatures commonly used for long-term storage. In solution, the compound is susceptible to hydrolysis and to microbial growth if it is not handled aseptically. The C-terminal proline-rich extension appears to slow enzymatic cleavage relative to tuftsin, though quantitative degradation rates vary with the matrix and the conditions tested. Published stability data specific to Selank remain sparse.
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.
| Property | Value | Notes |
|---|---|---|
| Chemical class | Synthetic heptapeptide | Analog of the tetrapeptide tuftsin |
| Sequence | Thr-Lys-Pro-Arg-Pro-Gly-Pro | Reported consistently across pharmacopoeial descriptions |
| Appearance | White to off-white lyophilized powder | Typical form of research-grade material |
| Solubility | Freely soluble in water | Aqueous buffers; poor in nonpolar solvents |
| Typical storage temperature | -20 degrees Celsius | Lyophilized powder; protect from moisture |
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.
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.
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.
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== Structure == The activin and inhibin protein complexes are both dimeric in structure, and, in each complex, the two monomers are linked to one another by a single disulfide bond. In addition, both complexes are derived from the same family of related genes and proteins but differ in their subunit composition. Below is a list of the most common inhibin and activin complexes and their subunit composition:
=== Vaccines === When pseudouridine is used in place of uridine in synthetic mRNA, the modified mRNA molecule arouses less response from Toll-like receptors, a part of the human immune system that would otherwise identify the mRNA as unwelcome. This makes pseudouridine useful in mRNA vaccines, including the mRNA COVID-19 vaccines. This property of pseudouridine was discovered by Katalin Karikó and Drew Weissman in 2005, for which they shared the 2023 Nobel Prize in Physiology or Medicine. N1-Methylpseudouridine provides even less innate immune response than Ψ, as well as improving translation capacity. Both Pfizer-BioNTech and Moderna mRNA vaccines therefore use N1-Methylpseudouridine rather than Ψ.
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=== Ending manufacture === Citing health concerns, several manufacturing companies have ended or stated that they plan to end the sale of PFAS or products that contain them. These companies include W. L. Gore & Associates (the maker of Gore-Tex), Patagonia, REI, H&M, and 3M. An alternative for some companies may have been to move production to countries such as Thailand and India, where there is less regulation.
=== Determining the time of divergence in phylogenetic trees === The molecular clock hypothesis predicts that the rate of amino acid substitution in a particular protein will be approximately constant over time, though this rate may vary between protein families. This suggests that the number of mutations per amino acid in a protein increases approximately linearly with time. Determining the time at which two proteins diverged is an important task in phylogenetics. Fossil records are often used to establish the position of events on the timeline of the Earth's evolutionary history, but the application of this source is limited. However, if the rate at which the molecular clock of protein family ticks — that is, the rate at which the number of mutations per amino acid increases — is known, then knowing this number of mutations would allow the date of divergence to be found. Suppose the date of divergence for two related proteins, taken from organisms living today, is sought. The two proteins have both been accumulating accepted mutations since the date of divergence, and so the total number of mutations per amino acid separating them is approximately twice that which separates them from their common ancestor. If a range of PAM matrices are used to align two proteins that are known to be related, then the value of
== Capillary electrochromatography == Capillary electrochromatography (CEC) is an electrochromatography technique in which the liquid mobile phase is driven through a capillary containing the chromatographic stationary phase by electroosmosis. It is a combination of high-performance liquid chromatography and capillary electrophoresis. The capillaries is packed with HPLC stationary phase and a high voltage is applied to achieve separation is achieved by electrophoretic migration of the analyte and differential partitioning in the stationary phase.
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In return, the host provides the symbiont with chemicals required for chemosynthesis, such as carbon, sulfide, and oxygen. In the early stages of studying life at hydrothermal vents, there were differing theories regarding the mechanisms by which multicellular organisms were able to acquire nutrients from these environments, and how they were able to survive in such extreme conditions. In 1977, it was hypothesized that the chemoautotrophic bacteria at hydrothermal vents might be responsible for contributing to the diet of suspension-feeding bivalves. Finally, in 1981, it was understood that giant tubeworm nutrition acquisition occurred as a result of chemoautotrophic bacterial endosymbionts. As scientists continued to study life at hydrothermal vents, it was understood that symbiotic relationships between chemoautotrophs and macrofauna invertebrate species was ubiquitous. For instance, in 1983, clam gill tissue was confirmed to contain bacterial endosymbionts; in 1984 vent bathymodiolid mussels and vesicomyid clams were also found to carry endosymbionts. However, the mechanisms by which organisms acquire their symbionts differ, as do the metabolic relationships. For instance, tubeworms have no mouth and no gut, but they do have a "trophosome", which is where they deal with nutrition and where their endosymbionts are found. They also have a bright red plume, which they use to uptake compounds such as O, H2S, and CO2, which feed the endosymbionts in their trophosome.
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Selank is a synthetic seven-amino-acid peptide modeled on tuftsin, a fragment of the immunoglobulin G heavy chain. It was designed in Russia to combine anxiolytic and immunomodulatory properties in one molecule.
The first four residues of Selank reproduce the tuftsin sequence Thr-Lys-Pro-Arg. A Pro-Gly-Pro extension at the C-terminus was added to slow enzymatic breakdown and extend residence time.
It holds marketing authorization in Russia, where nasal drop formulations are sold. No equivalent approval exists in the European Union, the United States, or most other countries.
The most common approach combines reverse-phase liquid chromatography with mass spectrometry. Chromatography separates the components while mass spectrometry confirms the molecular mass. Peptide sequencing or tandem mass analysis can further verify the amino acid order.