tuftsin is one of those subjects where the details matter more than the headlines. This page pulls together the background, the mechanisms, and the practical points readers ask about most.
Last reviewed on 2026-06-12. Where a claim depends on a specific study, the study is described rather than over-claimed.
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.
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.
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.
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.
| Property | Value | Notes |
|---|---|---|
| Molecular formula | C33H57N11O9 | Derived from the seven-residue sequence |
| Molecular weight | About 751.9 g/mol | Average mass; the monoisotopic value is slightly lower |
| Residue count | Seven amino acids | Thr-Lys-Pro-Arg-Pro-Gly-Pro |
| Parent compound | Tuftsin (Thr-Lys-Pro-Arg) | Selank extends tuftsin at the C-terminus |
| Compound class | Synthetic short peptide | Studied in a research setting; not a licensed drug in most markets |
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 work on this peptide almost always uses intranasal delivery, with drops or a spray applied to the nasal mucosa. Some animal experiments have used subcutaneous or intraperitoneal injection, and a smaller number have compared routes directly. Oral administration is not a focus of the literature, because short peptides of this size are broken down by digestive enzymes and cross intestinal barriers poorly. How much of an intranasal dose reaches the bloodstream intact in humans remains an open question.
Animal studies have examined behaviour in tests of anxiety, memory retention and stress response, and several report changes in neurotrophic or neurotransmitter-related markers. The human evidence base is much smaller, consisting mainly of short trials conducted in Russia with limited reporting in English-language journals. Sample sizes are modest and outcome measures vary between studies, so the findings are best described as preliminary. Independent replication under modern trial standards has not been widely reported.
Outside its country of origin the compound is generally handled as a research chemical rather than an approved medicine. No regulatory approval from the United States Food and Drug Administration or the European Medicines Agency has been granted for human use. Identity and purity are normally checked by reverse-phase high-performance liquid chromatography, with mass spectrometry used to confirm the molecular mass. Lyophilised material is stored cold and desiccated, and repeated freeze-thaw cycles are avoided.
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.
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.
=== Thyroid gland === The thyroid gland develops from two different clusterings of embryonic cells. One part is from the thickening of the pharyngeal floor, which serves as the precursor of the thyroxine (T4) producing follicular cells. The other part is from the caudal extensions of the fourth pharyngobranchial pouches which results in the parafollicular calcitonin-secreting cells. These two structures are apparent by 16 to 17 days of gestation. Around the 24th day of gestation, the foramen cecum, a thin, flask-like diverticulum of the median anlage develops. At approximately 24 to 32 days of gestation the median anlage develops into a bilobed structure. By 50 days of gestation, the medial and lateral anlage have fused together. At 12 weeks of gestation, the fetal thyroid is capable of storing iodine for the production of TRH, TSH, and free thyroid hormone. At 20 weeks, the fetus is able to implement feedback mechanisms for the production of thyroid hormones. During fetal development, T4 is the major thyroid hormone being produced while triiodothyronine (T3) and its inactive derivative, reverse T3, are not detected until the third trimester.
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== Antideuterium and the antideuteron == An antideuteron is the antimatter counterpart of the deuteron, consisting of an antiproton and an antineutron. The antideuteron was first produced in 1965 at the Proton Synchrotron at CERN and the Alternating Gradient Synchrotron at Brookhaven National Laboratory. A complete atom, with a positron orbiting the nucleus, would be called antideuterium, but as of 2019 antideuterium has not yet been created. The symbol used for antideuterium is D, that is, D with an overbar.
Sources: en.wikipedia.org
=== Introductory === Nelson DL, Cox MM (2004). Lehninger Principles of Biochemistry (4th ed.). W. H. Freeman. ISBN 0-7167-4339-6. Schneider ED, Sagan D (2006). Into the Cool: Energy Flow, Thermodynamics and Life (1st ed.). University of Chicago Press. ISBN 0-226-73937-6. Lane N (2006). Power, Sex, Suicide: Mitochondria and the Meaning of Life (1st ed.). Oxford University Press, USA. ISBN 0-19-920564-7.
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== Research and career == Parsons joined King's College London as a Royal Society University Research Fellow in 2005. She was promoted to Reader in 2013, and Professor in 2015. Parsons investigates the fundamental mechanisms that drive cell adhesion and migration using microscopy, molecular biology and three-dimensional simulations. She uses a confocal super-resolution microscope and Total internal reflection fluorescence microscope to image dynamic events over long periods. Whilst adhesion is critical to normal cellular function (e.g. development and homeostasis), it also drives cancer and fibrosis. In particular, Parsons focuses on integrins, and their behaviour in the extracellular matrix. By comparing "normal" cells with cancer cells, Parsons identified that the likelihood of cell invasion depended on the duration and chemistry of their adhesion with the matrix. Beyond fundamental cellular processes, Parsons has studied wound healing and inflammation using skin and lung epithelial cells. Parsons founded UKRI Technology Touching Life Integrated Biological Imaging Network, a multi-university, multidisciplinary research effort focussed on the development of strategies to understand and combat human disease. The network looks to understand the signalling hierarchy of cell adhesion, the molecular cues that regulate cell behaviour and the tissue mechanics that control cell growth. In 2017, Parsons was appointed to the executive committee of the Royal Microscopical Society. She is Editor in Chief of The International Journal of Biochemistry & Cell Biology.
=== Financing === In May 2016, Cerebras raised $27 million in a series A round led by Benchmark, Foundation Capital and Eclipse Ventures. In December 2016, the company raised a series B round led by Coatue Management. In January 2017, it raised a series C round led by VY Capital. In November 2018, Cerebras raised $88 million in a series D round, making the company a unicorn. Investors in this round included Altimeter, VY Capital, Coatue, Foundation Capital, Benchmark, and Eclipse. In November 2019, Cerebras raised $270 million in a series E round at a valuation of $2.4 billion. In November 2021, Cerebras raised $250 million in a Series F round, valuing the company at over $4 billion and bringing its total financing to $720 million. The Series F financing round was led by Alpha Wave Ventures and Abu Dhabi Growth Fund (ADG). In July, August, and September 2024, the company raised $85 million in a series F-1 round, selling shares for $14.66 each. In September 2025, the company raised $1.1 billion in a Series G round, selling shares for $36.23 each, or a valuation of $8.1 billion. In January 2026, the company raised $1.0 billion in a Series H round, selling shares for $89.01 each. In this round, Benchmark invested $225 million, while Alpha Wave and funds managed by Fidelity Investments each invested $100 million. On May 14, 2026, the company became a public company via the largest U.S. technology initial public offering since 2019, raising $5.55 billion by selling 30 million shares at $185 each and opening on Nasdaq at $350, valuing the company at $95 billion.
Sources: en.wikipedia.org
=== Deltas === Parts of the protein may have fixed three-dimensional structure without regular structures. They should not be confused with disordered or unfolded segments of proteins or random coil, an unfolded polypeptide chain lacking any fixed three-dimensional structure. These parts are frequently called "deltas" (Δ) because they connect β-sheets and α-helices. Deltas are usually located at protein surface, and therefore mutations of their residues are more easily tolerated. Having more substitutions, insertions, and deletions in a certain region of a sequence alignment maybe an indication of some delta. The positions of introns in genomic DNA may correlate with the locations of loops in the encoded protein . Deltas also tend to have charged and polar amino acids and are frequently a component of active sites.
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== Applications == DNA constructs can be used to produce proteins, including both naturally occurring proteins and engineered mutant proteins. These proteins can be used to make therapeutic products, such as pharmaceuticals and antibodies. DNA constructs can also change the expression levels of other genes by expressing regulatory sequences such as promoters and inhibitors. Additionally, DNA constructs can be used for research such as creating genomic libraries, sequencing cloned DNA, and studying RNA and protein expression.
Sources: en.wikipedia.org
Selank is a synthetic heptapeptide with the sequence Thr-Lys-Pro-Arg-Pro-Gly-Pro, designed as a metabolically stabilized analogue of the endogenous tetrapeptide tuftsin. It has been studied mainly against anxiety-related and cognitive endpoints rather than as an approved medicine in most jurisdictions.
Tuftsin contains four residues, while selank carries an additional Pro-Gly-Pro segment at the carboxyl end. That extension is intended to reduce enzymatic cleavage. Comparative pharmacokinetic data in humans remain limited.
No single receptor target is widely accepted as the definitive mediator of the reported effects. Proposed contributors include GABAergic modulation, shifts in monoamine turnover, and altered neuropeptide degradation. The mechanism is treated in the literature as unresolved.
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.