Selank comes up often in conversation and rarely with the context attached. Here we lay out the basics in order, then work through the practical considerations.
Updated 2025-08-02. Numbers and descriptions here follow the published literature rather than marketing material.
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.
Selank is a hydrophilic peptide and dissolves readily in water and in aqueous buffers. The lyophilised powder is typically a white to off-white solid. Because short peptides are prone to hydrolysis and oxidation, handling benefits from limiting exposure to heat, moisture and strong light. Working solutions are commonly prepared in sterile water or saline, and repeated freeze-thaw cycles are avoided to reduce aggregation and loss of activity. These practices reflect general laboratory convention rather than published stability specifications.
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.
| Property | Value | Notes |
|---|---|---|
| Common route | Intranasal | Also injected in some animal work |
| Solubility class | Freely soluble in water | Solid form is hygroscopic |
| Typical storage | About -20 degrees Celsius | Keep desiccated and dark |
| Purity method | Reverse-phase HPLC | Reported as area percent |
| Confirmatory method | Mass spectrometry | Verifies expected molecular mass |
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.
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.
Tuftsin, the parent structure, is a naturally occurring immunomodulatory tetrapeptide released from the Fc region of immunoglobulin G by spleen enzymes. Selank extends this four-residue sequence with three additional amino acids. The stated rationale is that the added tail slows enzymatic breakdown and may influence receptor interactions. How the full heptapeptide behaves at the molecular level is not firmly established, and proposed mechanisms often involve indirect modulation of neurotransmitter or immune signaling rather than a single defined target.
Selank is a synthetic heptapeptide developed in Russia. Its sequence is Thr-Lys-Pro-Arg-Pro-Gly-Pro, a seven-residue chain built around the natural tetrapeptide tuftsin. Researchers at the Institute of Molecular Genetics of the Russian Academy of Sciences first described the compound in the mid-1990s. The design combined the tuftsin core with an added Pro-Gly-Pro tail, a modification intended to extend the molecule's stability in biological fluids. Published work on the peptide has appeared mainly in Russian-language journals.
Reported activity for Selank centers on anxiolytic and nootropic effects. Russian clinical reports describe use in anxiety and in cognitive or attention-related complaints. Most of this evidence comes from studies conducted by the same research groups that developed the peptide. Independent replication in other countries remains limited, and no major Western regulatory agency has approved the compound for any indication. The gap between local reports and external verification is a recurring point in discussions of the peptide.
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.
== Life and education == Christian Hackenberger grew up in Damme. He attended the Gymnasium Damme, where he obtained his Abitur in 1995. After completing his civil service, he studied chemistry at the Albert-Ludwigs-Universität in Freiburg (1996–1998) and the University of Wisconsin-Madison (M.S. with Samuel H. Gellman, 1998–1999), with support from the German Academic Scholarship Foundation. He pursued his doctoral studies at the RTWH Aachen (2000–2003), where he worked under Prof. Carsten Bolm as a Kekulé Fellow from the Fonds der Chemischen Industrie. During this time, he also worked as an editorial assistant in scientific journalism for the WDR broadcast "Quarks & Co". From 2003 to 2005 he was a DAAD Postdoctoral Fellow at the Massachusetts Institute of Technology under Prof. Barbara Imperiali. In 2005, Hackenberger founded his own research group at the Free University of Berlin in 2005 as an Emmy Noether Fellow. In 2011, he was appointed as W2 Professor of Bioorganic Chemistry at the Free University of Berlin as the first Plus 3 awardee from the Boehringer Ingelheim Foundation. In 2012, he became Leibniz-Humboldt Professor for Chemical Biology at the Leibniz Research Institute for Molecular Pharmacology and the Humboldt University of Berlin. In 2020, Hackenberger co-founded the Munich-based biotechnology company Tubulis, which specializes in developing antibody-drug conjugates. He has served as associate editor of the Royal Society of Chemistry's scientific journals Organic and Biomolecular Chemistry (2015–2023) and Chemical Science (since 2024).
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Sources: en.wikipedia.org
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Sources: en.wikipedia.org
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Several types of cells support an action potential, such as plant cells, muscle cells, and the specialized cells of the heart (in which occurs the cardiac action potential). However, the main excitable cell is the neuron, which also has the simplest mechanism for the action potential. Neurons are electrically excitable cells composed, in general, of one or more dendrites, a single soma, a single axon and one or more axon terminals. Dendrites are cellular projections whose primary function is to receive synaptic signals. Their protrusions, known as dendritic spines, are designed to capture the neurotransmitters released by the presynaptic neuron. They have a high concentration of ligand-gated ion channels. These spines have a thin neck connecting a bulbous protrusion to the dendrite. This ensures that changes occurring inside the spine are less likely to affect the neighboring spines. The dendritic spine can, with rare exception (see LTP), act as an independent unit. The dendrites extend from the soma, which houses the nucleus, and many of the "normal" eukaryotic organelles. Unlike the spines, the surface of the soma is populated by voltage activated ion channels. These channels help transmit the signals generated by the dendrites. Emerging out from the soma is the axon hillock. This region is characterized by having a very high concentration of voltage-activated sodium channels. In general, it is considered to be the spike initiation zone for action potentials, i.e. the trigger zone. Multiple signals generated at the spines, and transmitted by the soma all converge here.
Sources: en.wikipedia.org
Most published work uses intranasal application, either as drops or as a nasal spray. Injection routes appear in a smaller set of animal experiments. Oral use is uncommon in the literature because peptide breakdown and poor absorption limit this route.
Reported human trials are few, brief and originate mainly from one country. They describe effects on anxiety-related measures, but sample sizes are small and reporting is limited. The results are widely regarded as preliminary rather than confirmed.
Reverse-phase liquid chromatography is used to assess purity and separation of related impurities. Mass spectrometry confirms that the observed molecular mass matches the expected peptide. A certificate of analysis from the supplier is the usual document of record.
Dry powder is normally held at -20 degrees Celsius or below in a sealed, light-protected container with desiccant. Brief room-temperature handling during weighing is generally tolerated. Storage instructions vary between suppliers, so the accompanying certificate of analysis should be followed.