tuftsin raises a handful of sensible questions. This page answers them in order, starting with the fundamentals and moving to applications.
Reviewed 2026-06-07. Anything still debated is marked as such rather than presented as settled.
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 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.
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.
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.
| 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 |
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.
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.
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.
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.
Tests performed by SHIELD Illinois represent 12% of all SARS-CoV-2 tests in Illinois and more tests than 24 entire states. To achieve this, SHIELD Illinois ultimately grew from a team of 30 to over 300 employees and more than 1,000 contractors.
To adopt a functional three-dimensional shape, the polypeptide chain must first form a series of smaller underlying structures called secondary structures. The polypeptide chain in these secondary structures then folds to produce the overall 3D tertiary structure. Once correctly folded, the protein can undergo further maturation through different post-translational modifications, which can alter the protein's ability to function, its location within the cell (e.g. cytoplasm or nucleus) and its ability to interact with other proteins. Protein biosynthesis has a key role in disease as changes and errors in this process, through underlying DNA mutations or protein misfolding, are often the underlying causes of a disease. DNA mutations change the subsequent mRNA sequence, which then alters the mRNA encoded amino acid sequence. Mutations can cause the polypeptide chain to be shorter by generating a stop sequence which causes early termination of translation. Alternatively, a mutation in the mRNA sequence changes the specific amino acid encoded at that position in the polypeptide chain. This amino acid change can impact the protein's ability to function or to fold correctly. Misfolded proteins have a tendency to form dense protein clumps, which are often implicated in diseases, particularly neurological disorders including Alzheimer's and Parkinson's disease.
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Clathurellinae was split into three families: Borsoniidae (also including species from Turridae), Mitromorphidae and Clathurellidae (all previously lumped under the Turridae). Conorbiinae was raised to the rank of family Conorbidae, consisting of three genera: Artemidiconus da Motta, 1991, Benthofascis Iredale, 1936, and Conorbis Swainson, 1840. Mangeliinae and Oenopotinae were combined and raised to the rank of family Mangeliidae, which had previously been lumped in the Turridae). Raphitominae was raised to the rank of family Raphitomidae (also previously lumped in the Turridae). The classification by Bouchet et al. (2011) was based on mitochondrial DNA and nuclear DNA testing, and built on the prior work by J.K. Tucker & M.J. Tenorio (2009), but did not include fossil taxa. Molecular phylogeny, particularly with the advent of nuclear DNA testing in addition to the mDNA testing (testing in the Conidae initially began by Christopher Meyer and Alan Kohn), is continuing on the Conidae.
Gam-COVID-Vac is a viral vector vaccine based on two recombinant replication-defective human adenoviruses: Ad26 (serotype 26) and Ad5 (serotype 5) replicated in HEK 293 cells. The viruses contain the gene that encodes the full-length spike protein (S) of SARS-CoV-2 to stimulate an immune response. Adenoviral vectors for expression of the SARS-CoV-2 spike protein have also been used in two other COVID-19 vaccines. One is the Janssen COVID-19 vaccine, which uses the Ad26COV2 viral vector based on the human virus Ad26. For this vaccine, the cell line PER.C6 is used to replicate the vector. Another one, the Oxford–AstraZeneca COVID‑19 vaccine, uses chimpanzee adenovirus (ChAdOx1) as the vector. For both the Oxford-AstraZeneca COVID-19 and Gam-COVID-Vac vaccines the producer cells for the production of non-replicating adenoviral vectors were obtained from the HEK 293 cell line. Each dose of Gam-COVID-Vac contains (1.0 ± 0.5) × 1011 virus particles. Both Ad26 and Ad5 were modified to remove the E1 gene to prevent replication outside the HEK 293 cells. For the production of the vaccine, to propagate adenoviral vectors in which the E1 gene was deleted, HEK 293 cells are used, which express several adenoviral genes, including E1. However, although rare, homologous recombination between the inserted cellular sequence and the vector sequence can restore the replication capacity to the vector, with less than 100 replicating adenovirus particles per dose of the vaccine.
Sources: en.wikipedia.org
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=== Pair potentials versus many-body potentials === The potential functions representing the non-bonded energy are formulated as a sum over interactions between the particles of the system. The simplest choice, employed in many popular force fields, is the "pair potential", in which the total potential energy can be calculated from the sum of energy contributions between pairs of atoms. Therefore, these force fields are also called "additive force fields". An example of such a pair potential is the non-bonded Lennard-Jones potential (also termed the 6–12 potential), used for calculating van der Waals forces.
Sources: en.wikipedia.org
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.
Selank is a synthetic heptapeptide designed as a stabilized analog of the natural tetrapeptide tuftsin. It has been investigated mainly for anxiolytic and cognitive effects. It is not an approved pharmaceutical in most countries.