If you have been reading about Pineal peptide and want a single page that covers the useful parts, this is it: definitions, context, how it is studied, and the questions that come up repeatedly.
Updated 2025-10-19. Numbers and descriptions here follow the published literature rather than marketing material.
The compound is described in the literature as a derivative of epithalamin, a preparation obtained from bovine pineal tissue. Work on this peptide family was carried out mainly by a research group in Saint Petersburg beginning in the 1980s, and the substance was later registered for clinical use in Russia under the name Epitalon. Outside that region it is generally treated as a research chemical rather than an approved medicine. Statements about its biological activity rest on a relatively small number of studies, and independent replication remains limited.
In its supplied form epitalon is a white to off-white powder, usually lyophilized and often hygroscopic. It dissolves readily in water and in aqueous buffers, and it is commonly handled as the acetate or trifluoroacetate salt to improve stability during purification and drying. The amide backbone is labile in aqueous media, so solutions are less durable than the dry solid. Handling notes in the chemical literature therefore emphasize keeping the powder dry, cool and shielded from light until it is dissolved.
Identity is normally established by reversed-phase high-performance liquid chromatography combined with mass spectrometry, a pairing that separates components and confirms molecular mass at once. Purity is quoted as a percentage from the chromatogram, and figures above ninety-five percent are a frequent commercial specification. Amino acid analysis or sequencing supplies further confirmation when required. Because many short peptides behave similarly under chromatography, retention time alone does not establish sequence; the mass measurement is what separates one tetrapeptide from another, and certificates should report both.
Short peptides such as AEDG are normally supplied as a freeze-dried solid and are kept dry, cold, and shielded from light. Holding at minus twenty degrees Celsius is common for the long term, while a refrigerator suffices for brief periods before use. The material takes up moisture to some degree, so containers should stay sealed and be allowed to reach room temperature before opening, which limits condensation on the contents. Repeated warming and cooling of a single container is discouraged because it admits water and can lower the amount of intact peptide.
Dissolution is usually performed in water or a suitable aqueous buffer, and the resulting liquid is divided into single-use portions before freezing. Freeze-thaw cycling is a recognised source of loss for short peptides, since each cycle can encourage aggregation or adsorption onto container walls. Working solutions are generally kept cold and used within a short window, although published stability data specific to epitalon are thin. Containers should be marked with concentration and date, and solutions examined for cloudiness before use.
| Property | Value | Notes |
|---|---|---|
| Chemical class | Synthetic tetrapeptide | Four residues, linear chain |
| Residue sequence | Ala-Glu-Asp-Gly | Single-letter form AEDG |
| Calculated mass | 390.3 daltons | Value for the free, uncharged form |
| Appearance | White to off-white powder | Usually supplied lyophilized |
| Solubility | Freely soluble in water | Often handled as a salt form |
The compound is generally described as a synthetic analogue of a fragment isolated from a pineal gland extract. Researchers associated with the Saint Petersburg Institute of Bioregulation and Gerontology introduced it during the 1980s and 1990s while studying short peptides from animal tissue. The original extract, called epithalamin, is a heterogeneous mixture, whereas epitalon is a single defined sequence. That distinction matters because findings reported for the extract are not automatically findings about the pure tetrapeptide, and claims about broader biological effects remain a separate question from the chemical identity described here.
Residue composition is the property that most cleanly separates verified material from mislabelled samples. Alanine, glutamate, aspartate and glycine appear in that order from the N-terminus, and the two acidic residues sit in the middle of the chain. Because the peptide is short, it can be produced by solid-phase synthesis and characterised by mass spectrometry without ambiguity. Any reported sample whose measured mass departs substantially from 390 daltons is a different compound or a degraded mixture rather than epitalon.
Storage practice centres on limiting moisture, oxygen, and repeated temperature cycling. Freeze-dried powder is generally held desiccated at minus twenty degrees Celsius or colder and protected from light. Reconstituted solutions are markedly less stable, and the aspartate-glycine junction is prone to succinimide formation at neutral to mildly alkaline pH. Portioning material into single-use aliquots reduces degradation compared with repeated freeze-thaw cycles. Stability data specific to this tetrapeptide remain scarce, so most handling guidance is extrapolated from general peptide chemistry rather than measured directly.
Documentation accompanying research peptides usually includes a certificate of analysis listing the batch number, purity figure, and test methods applied. Buyers comparing suppliers should check whether the reported purity refers to chromatographic area or to a mass-balance calculation, because the two are not equivalent. Counter-ion content, residual solvents, and water content are sometimes omitted from such certificates even though they affect the actual peptide mass present. Independent verification through a second laboratory is the most direct way to confirm that a supplied material matches its label.
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== Applications == Despite the reduced efficiency verses reversed phase HPLC, hundreds of applications have been reported using MLC. One of the most advantageous is the ability to directly inject physiological fluids. Micelles have an ability to solubilize proteins which enables MLC to be useful in analyzing untreated biological fluids such as plasma, serum, and urine. Martinez et al. found MLC to be highly useful in analyzing a class of drugs called b-antagonists, so called beta-blockers, in urine samples. The main advantage of the use of MLC with this type of sample, is the great time savings in sample preparation. Alternative methods of analysis including reversed phase HPLC require lengthy extraction and sample work up procedures before analysis can begin. With MLC, direct injection is often possible, with retention times of less than 15 minutes for the separation of up to nine b-antagonists. Another application compared reversed phase HPLC with MLC for the analysis of desferrioxamine in serum. Desferrioxamine (DFO) is a commonly used drug for removal of excess iron in patients with chronic and acute levels. The analysis of DFO along with its chelated complexes, Fe(III) DFO and Al(III) DFO has proven to be difficult at best in previous attempts. This study found that direct injection of the serum was possible for MLC, verses an ultrafiltration step necessary in HPLC. This analysis proved to have difficulties with the separation of the chelated DFO compounds and with the sensitivity levels for DFO itself when MLC was applied.
Indeed, evaluating such predictions often requires a structural alignment between the model and the true known structure to assess the model's quality. Structural alignments are especially useful in analyzing data from structural genomics and proteomics efforts, and they can be used as comparison points to evaluate alignments produced by purely sequence-based bioinformatics methods. The outputs of a structural alignment are a superposition of the atomic coordinate sets and a minimal root mean square deviation (RMSD) between the structures. The RMSD of two aligned structures indicates their divergence from one another. Structural alignment can be complicated by the existence of multiple protein domains within one or more of the input structures, because changes in relative orientation of the domains between two structures to be aligned can artificially inflate the RMSD.
=== Full scan MS === When collecting data in the full scan mode, a target range of mass fragments is determined and put into the instrument's method. An example of a typical broad range of mass fragments to monitor would be m/z 50 to m/z 400. The determination of what range to use is largely dictated by what one anticipates being in the sample while being cognizant of the solvent and other possible interferences. A MS should not be set to look for mass fragments too low or else one may detect air (found as m/z 28 due to nitrogen), carbon dioxide (m/z 44) or other possible interference. Additionally if one is to use a large scan range then sensitivity of the instrument is decreased due to performing fewer scans per second since each scan will have to detect a wide range of mass fragments. Full scan is useful in determining unknown compounds in a sample. It provides more information than SIM when it comes to confirming or resolving compounds in a sample. During instrument method development it may be common to first analyze test solutions in full scan mode to determine the retention time and the mass fragment fingerprint before moving to a SIM instrument method.
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Sources: en.wikipedia.org
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== Symbol encoding in character sets == The official symbol for the SI prefix micro is a Greek lowercase mu (μ). For reasons stemming from its design, Unicode has two different character codes for the letter, with slightly different appearance in some computer fonts, although most fonts use the same glyph. U+03BC μ GREEK SMALL LETTER MU is in the Greek range. According to The Unicode Consortium, the Greek letter character is preferred, but implementations must recognize the micro sign as well, for compatibility with legacy character sets. This distinction also occurs in some legacy code pages, notably Windows-1253. In circumstances in which only the Latin alphabet is available, ISO 2955 (since 1974, withdrawn 2001), DIN 66030 (since 1980) and BS 6430 (since 1983) allow the prefix μ to be substituted by the letter ⟨u⟩ (U+0075 u LATIN SMALL LETTER U) as, for example, in um for μm, or uF for μF . Similarly, capacitor values according to the RKM code defined in IEC 60062 (since 1952) can be written as 4u7 (or 4U7) instead of 4μ7 if the Greek letter μ is not available. The CJK Compatibility block contains square forms of some Japanese katakana measure and currency units. U+3343 ㍃ SQUARE MAIKURO corresponds to マイクロ maikuro.
Sources: en.wikipedia.org
The peptide contains four residues in the order alanine, glutamate, aspartate and glycine, abbreviated AEDG. The chain is linear and held together by three peptide bonds. Its calculated mass for the uncharged free form is about 390.3 daltons.
Epithalamin refers to a crude preparation derived from bovine pineal tissue, which contains many components. Epitalon is a single synthetic tetrapeptide identified from that material and produced by chemical synthesis. The two names are sometimes confused because early reports treated the synthetic peptide as an active fragment of the extract.
It has been registered for clinical use in Russia, where it is associated with a small family of short peptides. In most other jurisdictions it is not an approved medicine and is traded as a research chemical. Regulatory status varies by country and changes over time.
Reversed-phase high-performance liquid chromatography is run alongside mass spectrometry. The chromatogram separates components and gives a purity figure, while the mass spectrum confirms that the measured molecular mass matches the expected sequence. Neither measurement on its own is treated as sufficient.