Pinealon

Pinealon Research Peptide: Comprehensive Laboratory Guide

For professional laboratory research only. Not for human or veterinary use. Not for food, cosmetic, household, diagnostic, or therapeutic use.

Overview

Pinealon research peptide is the short, sequence-defined tripeptide L-glutamyl-L-aspartyl-L-arginine, commonly abbreviated Glu-Asp-Arg or EDR. Public chemical databases describe the parent molecule as a linear peptide with free amino and carboxyl termini, a neutral-form molecular formula of C₁₅H₂₆N₆O₈, and an average molecular mass of approximately 418.41 g/mol.^[1][2] The name “Pinealon” originated in a literature stream concerning ultrashort peptide bioregulators. It should be treated as a common or research name, not as proof of source, biological specificity, regulatory status, or suitability for any particular experiment.

This catalog entry positions Pinealon research peptide as an analytical and in vitro research reagent. Reported research themes include oxidative-stress readouts, ERK1/2 signaling kinetics, cell viability, neuronal morphology, peptide–DNA association, and exploratory gene-expression models. Those themes remain preclinical. Much of the biological literature comes from a limited network of collaborating laboratories, several studies test more than one peptide, and some mechanistic conclusions combine experimental observations with molecular modeling. Independent replication is limited. No biological result should therefore be inferred from chemical identity alone, and no statement on this page establishes efficacy, safety, potency, target engagement, or clinical relevance.

Purchasers should define the exact material by its lot documentation. The free peptide, an acetate or trifluoroacetate salt, a hydrate, or material containing residual counterion can share the sequence name while differing in formula weight, assay value, ionic behavior, and chromatographic response. The lot-specific certificate of analysis (“CoA”), not a generic web description, must control identity, purity, peptide content, counterion status, storage conditions, and retest date.

Molecular identity

Identity values above describe the parent Glu-Asp-Arg structure in PubChem and ChEBI.^[1][2] They do not replace a lot-specific identity test. Formula and mass will differ when a counterion, solvate, isotopic label, terminal modification, or covalent tag is included.

Structural and physicochemical features

EDR contains two acidic side chains and one basic guanidinium side chain, in addition to ionizable free termini. Its protonation state is therefore strongly pH dependent. Although database structure records may display a zero formal charge for a neutral drawing, the dominant solution microspecies near neutral pH is expected to be anionic. Exact net charge, apparent isoelectric region, electrophoretic mobility, retention, and solubility depend on pH, ionic strength, counterions, and temperature. Researchers should measure rather than assume these properties in the actual assay buffer.

With no tryptophan, tyrosine, or phenylalanine residue, Pinealon research peptide has no strong aromatic ultraviolet chromophore. Routine reversed-phase HPLC monitoring will consequently rely mainly on low-wavelength peptide-bond absorbance, where buffers, solvents, gradients, and baseline drift can materially affect integration. Its small size and high polarity may also produce weak retention under a conventional C18 method. Appropriate alternatives include adjusted ion-pairing conditions, hydrophilic-interaction chromatography, mixed-mode chromatography, or ion-exchange separation, each qualified for the intended analytical purpose.

The molecule has three stereogenic amino-acid centers in the database-defined L configuration. Ordinary intact-mass LC–MS can confirm elemental composition within instrument tolerance but cannot, on its own, prove residue order, distinguish every isomer, establish all-L stereochemistry, or quantify total peptide content. Sequence confirmation may require tandem MS with a justified interpretation, comparison to a qualified reference, amino-acid analysis, or an orthogonal structural technique. Chiral or enzymatic methods may be needed when stereochemical purity is a critical quality attribute.

Several degradation or artifact pathways deserve consideration during method development. N-terminal glutamate can potentially cyclize to a pyroglutamyl species under conducive conditions; aspartyl chemistry can produce sequence-related isomers; peptide bonds can hydrolyze; and repeated pH or temperature excursions can shift the impurity profile. Adsorption to glass or plastic, metal-ion association, sodium or potassium adduct formation in MS, and matrix proteolysis can distort apparent recovery. The absence of cysteine, methionine, and aromatic residues narrows—but does not eliminate—oxidative or photochemical concerns.

Mechanistic and research themes: what the evidence does and does not show

Oxidative-stress and viability readouts

A 2011 cell-culture study reported that EDR was associated with lower reactive-oxygen-species signals in rat cerebellar granule cells, PC12 cells, and activated neutrophils under selected stress conditions. The same report described reduced propidium-iodide uptake, altered cell-cycle behavior, and delayed ERK1/2 activation.^[5] An earlier Russian-language paper evaluated several short peptides in hypoxia-related models and reported antioxidant-enzyme and excitotoxicity hypotheses for Pinealon.^[4]

These observations support reproducibility studies of redox-sensitive endpoints; they do not establish that EDR is a direct antioxidant, an ERK inhibitor, or a generally cytoprotective compound. Fluorescent ROS probes can respond to probe loading, esterase activity, light exposure, metal ions, cell number, and peptide–probe interactions. Propidium iodide is a membrane-integrity readout rather than a complete account of death mechanism. A strong design should pair ROS measurements with orthogonal endpoints, record cell density and baseline viability, test for assay interference in cell-free wells, and separate early signaling events from later survival effects.

Peptide–DNA association and proposed gene regulation

Fluorescence-label experiments in HeLa cells and in vitro oligonucleotide studies have been cited as evidence that several ultrashort peptides, including EDR, can reach intracellular compartments and interact with selected nucleic-acid sequences.^[3] A later biophysical study used spectroscopy, NMR, viscometry, and molecular dynamics to examine EDR with DNA, reporting partial major-groove association and sensitivity to mono- and divalent ions, particularly magnesium-mediated screening of DNA phosphate charge.^[6]

These are valuable hypotheses for cell-free binding research, but “DNA association” should not be equated with sequence-specific transcriptional control in a living cell. Fluorescent conjugation may change charge, hydrophobicity, localization, and uptake. Experiments with purified DNA omit chromatin, competing proteins, nucleases, transport barriers, and intracellular peptide degradation. Molecular-dynamics and docking results identify plausible conformations, not measured occupancy or functional causality. Any promoter hypothesis should be tested with native peptide, direct target-engagement methods, sequence controls, chromatin-aware assays, perturbation experiments, and predefined criteria for replication.

Neuronal morphology and plasticity models

A 2021 publication examined EDR and KED in amyloid-related culture and transgenic mouse models, reporting differences in dendritic-spine measures and proposing promoter associations by computational docking.^[7] A 2025 correction states that two figures in the original article were duplicates described differently; the authors reported that the conclusions were unchanged. That correction should be reviewed alongside the paper. The animal findings are historical evidence context only and do not define an intended use for this catalog material.

A 2024 in vitro study using directly reprogrammed neurons derived from older-donor fibroblasts reported increased dendritic arborization across the short peptides tested. For EDR, the numerical reduction in an oxidative-DNA-damage readout narrowly missed statistical significance. The study also reported no detected effect of the tripeptides on mitochondrial activity, lysosomal activity, or p16 in that model.^[9] The null findings are important: they argue against collapsing diverse cellular endpoints into a broad “anti-aging” mechanism. Donor number, reprogramming state, image-analysis segmentation, culture maturity, batch effects, and the use of a single experimental system all affect generalizability.

Overall evidence boundary

A 2020 narrative review assembles proposed EDR relationships involving ERK signaling, apoptotic proteins, antioxidant systems, transcription factors, serotonin-associated biology, and calmodulin.^[8] That article is useful as a map of hypotheses, not as confirmation that all listed pathways are direct targets. Across this literature, terms such as “neuroprotective,” “epigenetic,” and “bioregulator” often summarize observed associations or author interpretations. They are not validated product specifications. No receptor, binding constant in a physiologically representative system, universal cellular uptake mechanism, or translation to clinical benefit can be considered established from the cited record.

Appropriate nonclinical applications

Within a qualified laboratory and subject to institutional biosafety and chemical-risk review, this material may be considered for:

• LC–MS, HPLC, capillary-electrophoresis, or mixed-mode method development for a highly polar tripeptide;
• reference-spectrum generation, fragmentation mapping, adduct assessment, and matrix-recovery studies;
• cell-free peptide–oligonucleotide association experiments using orthogonal biophysical techniques;
• in vitro assay-development work on oxidative-stress probes, cell integrity, or time-resolved ERK phosphorylation;
• in vitro neuronal or neuron-like cell morphology studies with automated, blinded image analysis;
• exploratory transcript, protein, or chromatin readouts designed to challenge specific gene-regulation hypotheses;
• stability, adsorption, proteolysis, and recovery studies in defined laboratory buffers or culture matrices; and
• comparison of native EDR with scrambled-sequence, amino-acid-mixture, counterion-matched, or labeled controls.

These applications are suggestions for analytical and in vitro research planning, not validated protocols. This material is not offered for experiments involving administration to a person or animal, for diagnostic decisions, or for any consumer-facing use.

Analytical quality control

A credible specification separates identity, chromatographic purity, and content. They are not interchangeable. A single HPLC area percentage can show the relative integrated signal under one method, but it does not prove sequence, absolute mass in the container, absence of non-UV-active impurities, or amount of water and counterion. For Pinealon research peptide, a scientifically useful release package should address the following attributes:

• Identity: intact-mass LC–MS or high-resolution MS matched to the declared chemical form, with acceptance limits, representative spectrum, charge/adduct assignments, and traceable raw-data identifiers.
• Sequence/structure: justified MS/MS, comparison to a qualified reference, or another orthogonal approach capable of addressing residue order. Where critical, assess stereochemical identity separately.
• Purity and related substances: a stability-indicating separation with stated column, mobile phases, gradient, detector wavelength, integration rules, system suitability, and reporting threshold. Because EDR is small and polar, demonstrate adequate retention and separation rather than relying on a generic peptide method.
• Net peptide content: quantitative amino-acid analysis, calibrated quantitative NMR, or another validated assay. Report this separately from HPLC area purity and from gross vial mass.
• Water and volatiles: Karl Fischer water where appropriate and residual-solvent testing suited to the manufacturing process.
• Counterion and inorganic residues: ion chromatography or an equivalent method for acetate, trifluoroacetate, chloride, or other declared ions; consider elemental or residue tests where synthesis and purification history warrants them.
• Microbiological attributes: endotoxin, bioburden, or mycoplasma testing only when relevant to the intended in vitro system. Such results do not establish sterility or suitability for administration.

Method performance should be fit for purpose. Specificity, range, accuracy, precision, detection or quantitation capability, and robustness should be demonstrated where applicable. ICH Q2(R2) provides a recognized framework for analytical-procedure validation, although use of that framework for a research reagent is voluntary and does not convert the material into a regulated medicinal product.^[10]

Experimental design considerations

1. Verify the test article. Record lot number, declared salt, peptide content, water, purity, and storage history. Confirm identity before interpreting a biological signal.
2. Define the causal question. Preselect a primary endpoint and distinguish binding, uptake, pathway modulation, morphology, and survival as separate questions. Avoid post hoc conversion of a broad screening signal into a mechanism.
3. Use informative controls. Include vehicle, untreated, positive-assay, counterion-matched, scrambled-sequence, and free-amino-acid-mixture controls where appropriate. An unrelated tripeptide can help identify nonspecific effects of charge or nutrient load.
4. Establish a concentration–response window in vitro. Begin with assay-compatibility and cytotoxicity range finding; include multiple concentrations and time points selected from pilot data. Do not infer a useful range in one system from a different cell type or publication.
5. Check exposure in the matrix. Measure peptide recovery and integrity over the experimental interval. Serum, conditioned medium, plastic binding, pH, and proteases may lower the concentration available to cells.
6. Control analytical interference. Run cell-free peptide-plus-reagent wells for fluorescent, luminescent, colorimetric, and redox assays. Confirm key findings with a chemically distinct readout.
7. Design for reproducibility. Use independent biological replicates, randomized plate positions, blinded image analysis, documented exclusion criteria, and a statistical plan that distinguishes technical from biological replication.
8. Test mechanism directly. For a proposed pathway, combine temporal ordering, target engagement, loss-of-function or blockade, and rescue logic. A change in transcript abundance or docking score alone is not proof of direct regulation.

Laboratory handling and storage

Handle as a research chemical of incompletely characterized toxicology. Use trained personnel, appropriate personal protective equipment, a task-specific risk assessment, and the current safety data sheet. Avoid inhalation of dry powder, aerosol generation, ingestion, and contact with skin or eyes. Keep work surfaces and weighing tools controlled to prevent cross-contamination.

Follow the lot label and CoA for storage. In the absence of a validated lot-specific stability study, keep dry material tightly sealed, protected from moisture and light, and at the conservative low temperature specified by the supplier. Allow a sealed container to equilibrate before opening to reduce condensation. Minimize open-container time. For analytical solutions, use a documented laboratory-grade solvent and buffer selected for the method; record pH and actual peptide content. Low-binding vessels may improve recovery. Prepare only the quantity required for the planned study, use aliquots where appropriate, and avoid repeated freeze–thaw cycles.

Do not assign a universal solution shelf life. Establish stability in the exact solvent, container, temperature, and matrix by a stability-indicating method. Inspect for unexpected precipitation or appearance changes, but do not treat visual clarity as proof of chemical integrity. Dispose of unused material and contaminated consumables according to institutional procedures and applicable local requirements.

Frequently asked questions

1. What is Pinealon research peptide?

It is the common research name for the linear L-amino-acid tripeptide H-Glu-Asp-Arg-OH, abbreviated EDR. The product name does not by itself define counterion, hydration, purity, content, or suitability; those are lot-specific attributes.

2. Is this material intended for people or animals?

No. It is supplied solely for analytical, biochemical, and in vitro laboratory research. It is not intended for human or veterinary use, administration, compounding, consumption, diagnosis, prevention, or treatment.

3. Are the formula and molecular mass always C₁₅H₂₆N₆O₈ and 418.407 g/mol?

Those values describe the neutral, unsolvated free parent peptide. A salt, hydrate, solvate, isotope label, tag, or terminal modification changes the complete material formula and mass. Always calculate from the form declared on the CoA.

4. Does a high HPLC purity value mean the container holds the labeled amount of peptide?

No. HPLC area purity is a relative result under one chromatographic and detection method. Net peptide content must account for water, counterions, salts, residual solvents, and non-detected material and should be established by a suitable quantitative assay.

5. Is there an established molecular mechanism for EDR?

No single mechanism is conclusively established. Published work reports associations involving redox readouts, ERK kinetics, intracellular localization, DNA interaction, gene-expression hypotheses, and neuronal morphology. Direct targets, native-peptide uptake, causal sequence specificity, and independent replication remain important open questions.

6. Which research systems are most appropriate?

Fit-for-purpose analytical methods, cell-free binding systems, and well-controlled in vitro cellular assays are appropriate starting points. Experimental design should include identity verification, sequence and matrix controls, interference testing, and orthogonal endpoints. This catalog material is not intended for live-animal studies.

7. How should the peptide be stored after solution preparation?

There is no universal answer. Stability depends on pH, buffer, ionic strength, matrix, container, temperature, and time. Follow any lot-specific data, minimize solution age and freeze–thaw exposure, and confirm integrity and recovery with a stability-indicating analytical method.

Related research materials

• Humanin — a mitochondrial-derived peptide material for comparative cellular-stress and neurobiology research.
• MOTS-c — a mitochondrial-derived peptide material for metabolic-signaling and cellular-stress models.
• SS-31 — a mitochondria-targeting tetrapeptide material for cardiolipin and bioenergetics research.
• Semax — an ACTH-derived synthetic peptide material for controlled neurobiology and signaling studies.
• Selank — a synthetic short-peptide material for comparative neuropeptide and immune-signaling models.
• DSIP — a nonapeptide material for analytical, sleep–wake, and circadian research models.
• Epithalon — the AEDG tetrapeptide material for comparative short-peptide and gene-expression research.
• Vilon — a Lys-Glu dipeptide material for comparative bioregulator and cell-signaling studies.
• Cartalax — a short-peptide material for comparative extracellular-matrix and cell-culture research.
• Thymalin — a peptide-mixture research material for comparative bioregulator assays.

Quality documentation for B2B review

Before purchase or release into a study, request a lot-specific CoA that identifies the manufacturer or testing laboratory, batch number, sequence, termini, salt/counterion, analytical methods, numerical results, acceptance criteria, test dates, approval signature, storage condition, and retest or expiry basis. Supporting records may include representative HPLC/UPLC chromatograms, raw or processed MS spectra, peptide-content data, water and counterion results, residual-solvent results, and method or reference-standard traceability.

Where required by the buyer’s quality system, also request an SDS, country and route of manufacture, synthetic-versus-biological origin statement, change-control policy, deviation history, and chain-of-custody information. Claims such as “research grade,” “high purity,” “GMP,” or “sterile” should be accepted only when their scope and supporting evidence are explicit. A certificate generated for one batch cannot substantiate another batch, and a third-party chromatogram without sample traceability cannot establish the identity of material in a supplied container.

References

1. National Center for Biotechnology Information. PubChem Compound Summary: Glu-Asp-Arg, CID 10273502. Official chemical identity and computed properties record.
2. European Bioinformatics Institute. ChEBI:156374 — Glu-Asp-Arg. Curated tripeptide identity, formula, mass, stereochemistry, and synonyms.
3. Fedoreyeva LI, Kireev II, Khavinson VKh, Vanyushin BF. Penetration of short fluorescence-labeled peptides into the nucleus in HeLa cells and in vitro specific interaction of the peptides with deoxyribooligonucleotides and DNA. Biochemistry (Moscow). 2011;76(11):1210–1219. PubMed PMID 22117547.
4. Kozina LS. Investigation of antihypoxic properties of short peptides. Advances in Gerontology. 2008;21(1):61–67. Russian-language article with English abstract. PubMed PMID 18546825.
5. Khavinson V, Ribakova Y, Kulebiakin K, et al. Pinealon increases cell viability by suppression of free radical levels and activating proliferative processes. Rejuvenation Research. 2011;14(5):535–541. PubMed PMID 21978084.
6. Silanteva IA, Komolkin AV, Morozova EA, Vorontsov-Velyaminov PN, Kasyanenko NA. Role of mono- and divalent ions in peptide Glu-Asp-Arg–DNA interaction. Journal of Physical Chemistry B. 2019;123(9):1896–1902. PubMed PMID 30762356.
7. Khavinson V, Ilina A, Kraskovskaya N, et al. Neuroprotective effects of tripeptides—epigenetic regulators in mouse model of Alzheimer’s disease. Pharmaceuticals. 2021;14(6):515. PubMed PMID 34071923. See also the 2025 correction, PMID 39861198.
8. Khavinson V, Linkova N, Kozhevnikova E, Trofimova S. EDR peptide: possible mechanism of gene expression and protein synthesis regulation involved in the pathogenesis of Alzheimer’s disease. Molecules. 2021;26(1):159. PubMed PMID 33396470. Narrative review; use as a hypothesis map rather than primary confirmation.
9. Kraskovskaya N, Linkova N, Sakhenberg E, et al. Short peptides protect fibroblast-derived induced neurons from age-related changes. International Journal of Molecular Sciences. 2024;25(21):11363. PubMed PMID 39518916.
10. U.S. Food and Drug Administration. Q2(R2) Validation of Analytical Procedures. Final guidance, March 2024.

Final research-use disclaimer

Pinealon research peptide is supplied exclusively as a laboratory research reagent. It is not a drug, medicine, supplement, food, cosmetic, diagnostic, or medical device. It is not approved or intended for use in humans or animals and must not be administered, compounded, consumed, or used to diagnose, prevent, mitigate, or treat any disease or condition. Biological findings summarized here are preclinical, model-specific, and subject to methodological limitations; they are provided to support research planning, not to promise an outcome. The purchaser is responsible for qualified personnel, lawful procurement, institutional approvals, safe handling, study design, waste disposal, and verification that the lot is fit for its intended in vitro or analytical purpose.