The short version of mass spectrometry fits in a sentence. The long version — which is the one that helps — is below.
Reviewed 2026-03-14. Anything still debated is marked as such rather than presented as settled.
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.
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.
Lyophilized Selank, the dry powder form, is generally stored frozen at minus 20 degrees Celsius or colder for long-term keeping. The solid is hygroscopic and should stay sealed, dry, and protected from light. Once dissolved, the peptide is less stable and is usually held refrigerated at 2 to 8 degrees Celsius for short periods. Repeated freezing and thawing is avoided because it can promote aggregation and loss of activity. Buffers and pH choice also affect how long a solution remains usable.
Solubility behavior is a practical concern for handling. Selank dissolves readily in water and in common aqueous buffers, which simplifies preparation of working solutions. The choice of solvent, ionic strength, and pH can influence aggregation over time, particularly at higher concentrations. Aqueous solutions are typically sterile-filtered before use. Because stability depends on several variables, storage and handling notes should be treated as general guidance rather than fixed rules, and specific values are best confirmed against a certificate of analysis for each batch.
| Property | Value | Notes |
|---|---|---|
| Chemical class | Synthetic heptapeptide | Tuftsin analogue with a C-terminal Pro-Gly-Pro tail |
| Amino acid sequence | Thr-Lys-Pro-Arg-Pro-Gly-Pro | Abbreviated TKPRPGP in most catalogues |
| Molecular mass | About 752 Da | Value for the free peptide |
| Solubility | Freely soluble in water | Aqueous solutions are kept cold and used promptly |
| Typical storage | -20 °C, dry, protected from light | Applies to the lyophilised powder before reconstitution |
Identity and purity of selank are established with reversed-phase high-performance liquid chromatography coupled to mass spectrometry. The peptide elutes from C18 columns with acetonitrile gradients in water containing trifluoroacetic acid or formic acid, and detection is usually performed by ultraviolet absorbance near 214 nm. Electrospray ionization in positive mode gives a doubly protonated ion near m/z 377, consistent with a mass of about 752 Da. Amino acid analysis or tandem mass spectrometry of fragment ions confirms the sequence. Because the molecule has no aromatic residues, it lacks a usable 280 nm chromophore, so low-wavelength detection or mass spectrometry is required.
Peptide bonds in selank are susceptible to hydrolysis under strongly acidic or basic conditions, and the terminal proline residues are vulnerable to exopeptidase activity in biological samples. Lyophilized powder stored dry at -20 °C typically remains stable for extended periods, whereas aqueous solutions degrade faster and may lose measurable purity within days to weeks depending on pH, temperature, and microbial load. Repeated freeze-thaw cycles promote aggregation and adsorption to container surfaces. For analytical work, solutions are usually prepared fresh, kept cold, and used within a single working day.
Handling follows standard practice for research peptides. Material is weighed in a low-humidity environment because the powder absorbs atmospheric moisture. Purity is reported as the percentage area of the main peak in a chromatogram, with specifications commonly set at 95 percent or higher; values below that threshold indicate the presence of truncated or modified species. Residual trifluoroacetate from purification is often present and may affect mass balance. Certificates of analysis should state the analytical method, the column and gradient used, and the lot-specific retention time so that results can be compared across suppliers.
Laboratory work relies on standard behavioral paradigms. Rodents are tested in the elevated plus maze, open field, and passive avoidance tasks, with outcomes compared against diazepam or vehicle controls. Intranasal dosing is used most often because it bypasses first-pass metabolism, though intraperitoneal and intravenous routes also appear in published protocols. Biochemical endpoints include tissue BDNF concentrations, cytokine levels, and monoamine metabolites. Human data are limited to small Russian trials reporting reduced anxiety scores; most were not prospectively registered, and few employed independent outcome assessment.
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.
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.
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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Tempeh begins with whole soybeans, which are softened by soaking, dehulled, then partly cooked. Specialty tempeh may be made from other types of beans, wheat, or may include a mixture of beans and whole grains. Adding vinegar during soybeans soaking process had also been reported in tempeh industries and it had been found to influence the sensory nature of the final product. The principal step in making tempeh is the fermentation of soybeans which undergo inoculation with Rhizopus spp. molds, a type of filamentous fungus most widely used for the production of tempeh. A fermentation starter containing the spores of fungus Rhizopus oligosporus or Rhizopus oryzae is mixed in. The beans are spread into a thin layer and are allowed to ferment for 24 to 36 hours at a temperature around 30°C (86°F). The soybeans have to cool down to allow spore germination and abundant growth of mycelium. Later, the temperature of the beans will naturally rise and rapid mold growth happens for around 4 hours. As mold growth declines, the soybeans should be bound into a solid mass by the mycelium. In good tempeh, the beans are knitted together by a mat of white mycelium. Typically, tempeh is harvested after 48 hours of fermentation with its distinguishable whitish color, firm texture, and nutty flavor. Extended fermentation time results in an increase in pH and undesirable color darkening in the tempeh.
===== Other names in the Western world ===== In the last decades, two new important terminologies emerged. Both are commonly used in the Western world in neoshamanic, recreative or pharmaceutical contexts to address ayahuasca-like substances created without the traditional botanical species, due to it being expensive and/or hard to find in these countries. These concepts are surrounded by some controversies involving ethnobotany, patents, commodification and biopiracy:
Testosterone can also be aromatized into estradiol (E2) to inhibit LH. E2 decreases pulse amplitude and responsiveness to GnRH from the hypothalamus onto the pituitary. Changes in LH and testosterone blood levels and pulse secretions are induced by changes in sexual arousal in human males.
Sources: en.wikipedia.org
P7C3 (pool 7, compound 3) is a drug related to latrepirdine (dimebon) which has neuroprotective and proneurogenic effects and may be potentially useful for the treatment of Alzheimer's disease and similar neurodegenerative disorders. The pharmacological effects of P7C3 in vitro resemble those of endogenous proneurogenic peptides such as fibroblast growth factor 1 (FGF-1), and the proneurogenic activity of P7C3 was around thirty times that of latrepirdine when they were compared in mice. P7C3 was chosen for further animal studies on the basis of favorable pharmacokinetic factors, such as its high oral bioavailability and long duration of action, but several other related compounds showed similar activity such as the more potent fluorinated analogue P7C3-A20 which is up to ten times stronger again, and the methoxy analogue P7C3-OMe, for which it was determined that the (R) enantiomer is the active form.
For scientific purposes, after 1906, Doyen combined 15 of his films into three compilations, two of which survive: the six-film series Extirpation des tumeurs encapsulées (1906), and the four-film Les Opérations sur la cavité crânienne (1911). These and five other of Doyen's films survive.
==== Fehling test ==== The Fehling test is a classic method for the detection of aldoses. Due to mutarotation, glucose is always present to a small extent as an open-chain aldehyde. By adding the Fehling reagents (Fehling (I) solution and Fehling (II) solution), the aldehyde group is oxidized to a carboxylic acid, while the Cu2+ tartrate complex is reduced to Cu+ and forms a brick red precipitate (Cu2O).
Sources: en.wikipedia.org
Selank is a seven-amino-acid peptide built from the tuftsin sequence plus a Pro-Gly-Pro tail. It is produced by chemical synthesis rather than extracted from a natural source. The free peptide is usually supplied as a lyophilised powder or in an aqueous formulation.
Tuftsin is a natural tetrapeptide derived from the Fc portion of immunoglobulin G. Selank retains that tetrapeptide at its N-terminus and adds three residues to improve resistance to enzymatic breakdown. The relationship is structural, and the two molecules are not interchangeable in experimental work.
It holds a product registration in Russia for intranasal use as an anxiolytic. Registrations of that kind are not automatically accepted by regulators elsewhere. In most other countries it is treated as an unapproved substance or a research material.
Reverse-phase HPLC is the usual method and gives a percentage purity value. Mass spectrometry then confirms the molecular mass. Together they provide a basic identity and purity profile for a lot.