This is a working overview of Selank, written for readers who want more than a one-paragraph summary but less than a textbook.
This page was last updated on 2026-03-20 and is reviewed periodically as new material appears.
The compound was designed at the Institute of Molecular Genetics of the Russian Academy of Sciences during the 1980s and 1990s. The stated design goal was to retain the immunomodulatory and central nervous system activity attributed to tuftsin while improving resistance to enzymatic breakdown. Adding a proline-rich tail to the short parent peptide was a deliberate strategy, because proline residues restrict the conformations available to many peptidases. The same laboratory produced Semax, an ACTH fragment analog, and both compounds were developed in parallel as short, enzymatically stabilized peptides intended for intranasal use.
Selank is not a naturally occurring peptide and has no known endogenous counterpart in human physiology. Russian-language sources frequently call it TP-7, while English-language sources use the name Selank almost exclusively. Database indexing is uneven, partly because early reports appeared in regional journals that are not widely cataloged. Some summaries describe the material as a tuftsin analog and others as a synthetic heptapeptide; the labels overlap rather than conflict. Citing the primary sequence resolves ambiguity more reliably than the research or trade name alone.
Selank is a synthetic heptapeptide with the sequence Thr-Lys-Pro-Arg-Pro-Gly-Pro, written TKPRPGP in one-letter notation. Its structure consists of the immunomodulatory tetrapeptide tuftsin, Thr-Lys-Pro-Arg, extended at the carboxyl terminus by a Pro-Gly-Pro segment. The molecular formula is commonly given as C33H57N11O9, corresponding to a monoisotopic mass near 751.4 Da and an average molecular mass near 751.9 Da. All seven residues are proteinogenic amino acids, and the molecule carries no modified side chains or non-natural linkages.
Measuring peptide exposure inside the brain is technically difficult. Selank is degraded rapidly in plasma, and assays must separate intact peptide from fragments, which favors targeted mass spectrometry over immunoassays alone. Reported half-lives are short, on the order of minutes, so effects observed hours later are attributed to downstream signaling rather than to the parent compound. Blood-brain barrier permeability is debated and rarely quantified directly. Gaps include absent dose-response characterization, inconsistent reporting of purity, and almost no pharmacokinetic data from human participants.
Selank is studied chiefly as an animal-model anxiolytic with proposed secondary effects on memory and immune signaling. Reported mechanisms include modulation of the GABA-A receptor complex, inhibition of enkephalin-degrading enzymes, and shifts in monoamine turnover within limbic structures. Some experiments describe increased expression of brain-derived neurotrophic factor in the hippocampus after repeated dosing. No single molecular target has been confirmed, and the peptide does not bind any receptor with the selectivity typical of a conventional small-molecule drug. Mechanism therefore remains a set of hypotheses rather than an established pathway.
| Property | Value | Notes |
|---|---|---|
| Peptide sequence | Thr-Lys-Pro-Arg-Pro-Gly-Pro | Seven residues; tuftsin plus a Pro-Gly-Pro tail |
| Molecular formula | C33H57N11O9 | Commonly reported value for the free peptide |
| Monoisotopic mass | Roughly 751.4 Da | Average molecular mass near 751.9 Da |
| Appearance | White to off-white powder | Typically supplied as a lyophilized solid |
| Solubility class | Freely soluble in water | Also dissolves in saline and other polar solvents |
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.
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.
Published clinical work is concentrated in Russian-language journals and generally involves small samples without independent replication. Systematic reviews in English note the shortage of randomised, placebo-controlled trials and the difficulty of verifying methods from translated reports. Outcome measures vary between studies, which complicates pooling of results. Interest in the compound as a cognitive or anxiolytic agent therefore rests on a thinner evidence base than the volume of citations suggests. Replication in well-powered trials with preregistered endpoints would be needed before firm conclusions about efficacy can be drawn.
Proposed mechanisms centre on the GABAergic system. Animal and tissue studies report changes in GABA-A receptor expression and reduced activity of GABA transaminase, the enzyme that degrades GABA. Effects on monoamine turnover, including serotonin and dopamine pathways, are also described, and a separate line of work links the peptide to increased expression of brain-derived neurotrophic factor in hippocampal tissue. Most of these findings come from rodent models and cell preparations. How the individual observations combine into a single coherent mode of action is not settled.
Dry powder is normally held at -20 degrees Celsius or lower, in a sealed container with desiccant and protection from light. Reconstituted solutions are usually kept at 2 to 8 degrees Celsius for short periods and frozen for longer ones. Proline residues at several positions are generally associated with some resistance to peptidase attack, but chemical stability still declines at neutral to alkaline pH and at elevated temperature. Exact shelf-life figures are product-specific and are not standardised across suppliers.
Identity and purity are usually assessed by reversed-phase high-performance liquid chromatography, with mass spectrometry used to confirm molecular mass and sequence information. Amino acid analysis and peptide mapping may supplement these methods. Certified reference standards are scarce, and many commercial lots are sold as research chemicals without a pharmacopoeial monograph. Regulatory treatment differs by country: Selank is a registered prescription medicine in Russia, while in the European Union and the United States it is not an approved drug and may fall under research-chemical or unapproved-product frameworks.
Multiplying by the molar mass constant ensures that the calculation is dimensionally correct: relative atomic masses and standard atomic weights are dimensionless quantities (i.e., pure numbers), whereas molar masses have units (in this case, grams per mole). Some elements are usually encountered as molecules, e.g. hydrogen (H2), nitrogen (N2), oxygen (O2), sulfur (S8), chlorine (Cl2). The molar mass of molecules of these elements is the molar mass of the atoms multiplied by the number of atoms in each molecule:
=== Ferdinand Schwarzwald === Ferdinand Schwarzwald (Nico Rogner) is the CFO of family-owned Austrian bank IBN Bauer, and a director on the board of Tender, in which his bank has a 6% stake. He backs Whitney's vision for pivoting the company away from pornography and gambling clients and into banking, and cautions Whitney that his co-founder and CEO Jonah Atterbury is "not a serious person", contributing to Jonah's eventual removal from the company. Ferdinand later helps Whitney and new Tender CEO Henry Muck execute a merger with IBN Bauer, traveling with them to Vienna to assuage the concerns of family heir Moritz-Hunter Bauer. He and Whitney also procure a billion-dollar investment from Al-Mi'raj Pierpoint during the release of Tender's banking app. Ferdinand is later revealed to be Whitney's handler on behalf of Russian foreign intelligence, having been recruited years ago by Cozy Bear (the hacker group affiliated with the FSB and SVR) and installed as IBN Bauer's CFO after stealing client lists that Russia could use as leverage. Amid public revelations of Tender's fraudulent profits out of Africa, Ferdinand warns Whitney that their narrative must remain intact, and implies that the Russians can assassinate anyone who goes "off-message". Ferdinand and fixer Dez Watkins later catch Whitney trying to disappear via New York and intercept him, forcing him to proceed with a hostile takeover bid for Pierpoint as it would represent a valuable "data set" for Russia.
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In Half-Life: Blue Shift, Rosenberg makes his first appearance during the Hazard Course tutorial, long before Calhoun encounters him in the train yards. He can be seen behind the observer's window during the duck-jump portion of the training. Sometime between Gina and Colette's last sight of Rosenberg in Decay and Calhoun's eventual rescue of the scientist in Blue Shift, he tries to enact an escape plan to get out of Black Mesa with the help of several other scientists. During this time, he is captured by soldiers and held captive in a freight car for questioning, while a colleague, Harold, is cornered and fatally wounded. Before Harold dies, Barney Calhoun discovers him, and he instructs Calhoun to find Dr. Rosenberg to help him with his plan. Calhoun is able to reach the train yards and free Dr. Rosenberg. Rosenberg informs him that their plan is to use the equipment in the prototype labs to teleport to safety. He leads Calhoun to the unused part of the complex where two other scientists, Walter Bennett and Simmons, are already preparing the machine. Rosenberg instructs Calhoun that he must activate and align a relay device on Xen in order for them to be able to accurately set their destination. Calhoun travels to Xen and is successful in accomplishing this task, but after returning through the portal back to Earth (it is here that Gina and Colette in Decay, temporarily caught in a harmonic reflux, hear Rosenberg's voice calling Calhoun through the portal), they discover that they need another power cell to replenish the teleporter's power for their escape.
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Sources: en.wikipedia.org
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Although Ginkgo biloba and other species of the genus were once widespread throughout the world, its habitat had shrunk by two million years ago. For centuries, it was thought to be extinct in the wild, but is now a common tree cultivated throughout eastern China, Korea, and Japan. Many municipalities in China, Korea and Japan use ginkgos as street trees, and ginkgo leaves are the emblem of prominent educational institutions such as the University of Tokyo and Sungkyunkwan University in South Korea. Despite their widespread habitat, high genetic uniformity exists among ginkgo trees, with some Chinese scholars suggesting that ginkgo trees in these areas may have been planted and preserved by Chinese monks over about 1,000 years. A study demonstrates a greater genetic diversity in Southwestern China populations, supporting glacial refugia in mountains surrounding the eastern Tibetan Plateau, where several old-growth candidates for wild populations have been reported. Whether native ginkgo populations still exist has not been demonstrated unequivocally, but there is genetic evidence that these Southwestern populations may be wild, as well as evidence that the largest and oldest G. biloba trees may be older than surrounding human settlements. Where it occurs in the wild, Ginkgo is found infrequently in deciduous forests and valleys on acidic loess (i.e. fine, silty soil) with good drainage. The soil it inhabits is typically in the pH range of 5.0 to 5.5.
Sources: en.wikipedia.org
The sequence is Thr-Lys-Pro-Arg-Pro-Gly-Pro, written TKPRPGP in one-letter code. It combines the tetrapeptide tuftsin with a carboxyl-terminal Pro-Gly-Pro extension. This full sequence identifies the molecule more precisely than the research name.
No peptide with this exact sequence has been identified as an endogenous substance. It is a laboratory-designed analog of tuftsin, a naturally occurring immunomodulatory tetrapeptide. The Pro-Gly-Pro extension has no known natural source.
Proline introduces conformational constraints that make a peptide less accessible to common peptidases. This is a standard stabilization strategy in peptide design. The added residues also increase the distance between the active tuftsin portion and typical cleavage sites.
Intranasal administration predominates in both animal and human research because it avoids hepatic first-pass metabolism. Injectable and intraperitoneal routes appear in animal work mainly for comparison.