Pinealon (EDR): Tripeptide Bioregulator Research Guide

Search for “pinealon” and you’ll find a strange gap. Dozens of comparison pages rank reasonably well for “pinealon vs semax” or “pinealon vs epithalon,” yet the compound’s own name barely shows up in the top results anywhere. That’s backwards for a peptide with an actual published literature behind it. This guide is our attempt to close that gap: what Pinealon (EDR) actually is, what the Khavinson group’s published work reports, and where the evidence stops.

Pinealon is a synthetic tripeptide with the sequence glutamate, aspartate, arginine, shortened to EDR using single letter amino acid codes. It came out of the peptide bioregulator research program run by Vladimir Khavinson’s group at the St. Petersburg Institute of Bioregulation and Gerontology. Published papers from that group describe EDR entering cell nuclei and interacting with specific DNA sequences, plus effects in central nervous system cell culture and animal models. We’re covering both here, along with the honest limitation that almost none of this work has been replicated outside the group that produced it. Available for laboratory research only.

What Pinealon Is

Start with the chemistry, since it’s simple and often skipped over. Pinealon is glutamic acid, aspartic acid, and arginine linked in that order: Glu-Asp-Arg, or EDR. Three amino acids. No branching, no modified residues, nothing exotic. That size matters for a lot of what follows, because a tripeptide behaves very differently from a 30 or 40 residue peptide in terms of stability, membrane crossing, and how easily it gets degraded once it’s in solution.

The compound sits inside a larger family Khavinson’s group calls peptide bioregulators. Each one is a short peptide, usually two to four amino acids, matched conceptually to a tissue of origin. Epithalon (Ala-Glu-Asp-Gly, AEDG) is the pineal gland peptide. Cortagen targets cerebral cortex tissue. Vesugen is associated with vascular tissue. Pinealon’s assigned tissue is the central nervous system broadly, not the pineal gland specifically, despite the name’s obvious echo of “pineal.” That naming choice trips people up. Epithalon is the pineal-derived one; Pinealon is the CNS-targeted one, and the two get confused in casual write-ups more often than you’d expect.

Where does the idea come from in the first place? Khavinson’s rationale traces back to older work on tissue extracts, Epithalamin among them, a polypeptide preparation derived from bovine pineal tissue that was studied in Russian aging research going back decades. The theory was that pineal and CNS tissue contain naturally occurring short peptides that carry some kind of regulatory signal specific to that tissue, and that synthesizing short fragments matching those sequences might reproduce part of the effect without needing a crude tissue extract. Pinealon is one of several synthetic tripeptides built on that premise, positioned as a cleaner, better-defined alternative to whole-extract preparations like Epithalamin.

Whether that theoretical framework holds up is a separate question from whether the specific experimental findings on Pinealon research peptide are real and worth examining. We think they’re worth examining. But it’s fair to flag upfront that the “tissue-specific regulatory peptide” idea is Khavinson’s interpretive lens on the data, not an independently established mechanism accepted broadly across peptide biology. Keep that separation in mind as we go through the actual findings.

The Peptide Bioregulator Framework

Here’s the hypothesis in plain terms. Khavinson’s group proposes that ultrashort peptides, two to four amino acids, can enter a cell nucleus and physically interact with DNA at specific sequence motifs, functioning as a kind of epigenetic switch that turns certain genes up or down. This is a stronger and more specific claim than “peptides can affect gene expression somehow.” It says these particular short sequences bind particular DNA regions and that binding has downstream transcriptional consequences.

That’s a hypothesis, not settled biology. Short peptide to DNA interaction of this kind isn’t part of mainstream molecular biology curricula, and most gene regulation research focuses on transcription factors, which are considerably larger proteins with well-characterized DNA-binding domains. A three or four amino acid chain interacting sequence-specifically with double-stranded DNA is an unusual claim on its face. It’s not impossible. Short peptide-nucleic acid interactions do exist in nature (certain antimicrobial peptides, some viral proteins use short motifs to engage nucleic acids), but the specificity and functional consequence Khavinson’s group describes for compounds like EDR is a much bigger ask.

So what’s the actual supporting evidence? The clearest piece comes from Fedoreyeva and colleagues, who used fluorescently labeled versions of several bioregulator peptides, including EDR, and tracked their movement into HeLa cell nuclei under a microscope. They then ran fluorescence quenching experiments to test whether the peptides bound labeled DNA oligonucleotides in vitro, and found that binding strength varied depending on the specific nucleotide sequence tested. EDR showed a binding preference for CAG-containing sequences, distinct from the binding pattern shown by Epithalon or bronchogen in the same experiment. That specificity, different peptides binding different sequence motifs, is the strongest piece of evidence for the “sequence-specific interaction” part of the hypothesis. It doesn’t prove a functional transcriptional consequence on its own, but it’s a real, replicable-in-principle biochemical observation, not just a claim.

Pinealon’s three-residue EDR sequence is the smallest of Khavinson’s bioregulator peptides. See the Cognitive Research Stack featuring Pinealon.

What about the mechanism connecting nuclear DNA binding to the downstream effects reported in cell cultures and animal models? That’s where things get thinner. The gene expression changes Khavinson’s group reports (serotonin pathway genes, antioxidant response genes, and others depending on the paper) are consistent with the DNA-binding hypothesis but don’t prove causation from it. Correlation between “peptide is present” and “certain genes changed expression” doesn’t establish that the peptide caused the change through direct DNA binding specifically, as opposed to some downstream signaling cascade the peptide triggered by another route entirely. The docking study we cover below is a computational prediction, not a direct biochemical demonstration of binding at that exact promoter site. Treat the whole framework as a working hypothesis with some genuinely interesting supporting data, not a proven mechanism.

One earlier paper from the group, published in Rejuvenation Research in 2011, is worth calling out because it directly tests the cell to genome interaction claim rather than just describing downstream effects. Khavinson, Ribakova, Kulebiakin, and colleagues found that Pinealon reduced reactive oxygen species accumulation and necrotic cell death, dose dependently, across three different cell types: cerebellar granule cells, neutrophils, and PC12 pheochromocytoma cells. They also tracked ERK 1/2 activation and cell cycle progression, and found the antioxidant effect saturated at lower peptide concentrations while cell cycle modulation kept scaling at higher doses. Two effects with two different dose response curves is the kind of detail that suggests two separate mechanisms rather than one effect wearing two hats, and the authors used exactly that logic to argue Pinealon interacts directly with the cell genome on top of its antioxidant activity (PMID 21978084).

What the Published Research Reports

We reviewed the primary papers behind the claims most commonly repeated about Pinealon online, and it’s worth being specific about which model system produced which finding, since a lot of secondary coverage blurs cell culture data into animal data into vague “studies show” language. Three papers carry most of the weight here.

The DNA Interaction Hypothesis

Fedoreyeva, Kireev, Khavinson, and Vanyushin published the foundational nuclear-penetration paper in Biochemistry (Moscow) in 2011. Working in HeLa cells (a human cervical cancer cell line, not neuronal tissue, which is a detail some secondary sources gloss over), they incubated cells with fluorescein-labeled short peptides, EDR among them, and observed fluorescence accumulating in the cytoplasm, the nucleus, and the nucleolus. That confirmed the peptides physically get inside the nucleus. The team then ran separate in vitro binding assays using fluorescence quenching to measure how strongly each peptide interacted with different single and double stranded DNA oligonucleotide sequences.

The result: EDR, along with epithalon and testagen, showed preferential binding to CAG-containing sequences, while bronchogen preferred CTG sequences. The peptides also appeared able to discriminate methylated versus unmethylated cytosine at CNG sites, which the authors flagged as potentially relevant to epigenetic regulation, since CNG methylation status affects gene expression in eukaryotic cells (PMID 22117547). This is a HeLa cell and in vitro biochemistry paper. It says nothing directly about neurons, and nothing about live animals. What it does establish, reasonably convincingly, is that this class of short peptide can enter nuclei and bind DNA with some sequence specificity. That’s the base the rest of the framework builds on.

Is that enough to call it settled? No. One paper, one lab, one cell line, no independent replication we could locate in the broader literature. The finding is specific enough (measurable quenching constants, distinct binding patterns across different peptides) that it doesn’t read like vague hand-waving, and the methodology (fluorescence quenching for nucleic acid binding) is a standard technique used elsewhere in biochemistry. Still, “used a standard technique” and “independently confirmed by another group” are different bars, and only the first one is cleared here.

The functional side of the hypothesis, that this DNA binding actually drives the neuroprotective and gene-expression effects described elsewhere in the literature, comes from Khavinson, Lin’kova, Tarnovskaya, and colleagues, published in the Bulletin of Experimental Biology and Medicine in 2014. Working in aging brain cortex cell cultures, they found that EDR and a related dipeptide, Lys-Glu-Asp, stimulated serotonin expression. Using molecular docking, a computational method for predicting how a small molecule fits against a target structure, they identified a CCTGCC sequence within the tryptophan hydroxylase gene (the enzyme that makes the rate-limiting step in serotonin synthesis) as a plausible binding site complementary to these peptides (PMID 24909721). The authors describe this as epigenetic regulation of serotonin synthesis with both neuroprotective and geroprotective (aging-related) relevance.

Two things worth flagging about that paper. First, “molecular docking suggests a binding site” is a prediction, not direct structural confirmation via something like crystallography or a gel shift assay. It’s a reasonable first step, not a final answer. Second, aging cell cultures are a specific and somewhat unusual model system; the serotonin finding is interesting but narrow, and it hasn’t (to our knowledge) been extended to a broader panel of aging-related genes to see how general the effect is.

The third major paper moves out of cell culture entirely and into an animal model. Arutjunyan, Kozina, Stvolinskiy, Bulygina, Mashkina, and Khavinson published a study in the International Journal of Clinical and Experimental Medicine in 2012 examining Pinealon in pregnant rats with diet-induced hyperhomocysteinemia (elevated homocysteine caused by excess dietary methionine, a model used to study prenatal metabolic stress and its effects on offspring neurodevelopment). Pinealon administration to the pregnant dams was associated with improved spatial orientation and learning ability in the offspring, along with reduced reactive oxygen species accumulation and fewer necrotic cells in cerebellum neurons isolated from the offspring (PMID 22567179). The authors describe the finding as consistent with earlier in vitro neuroprotective data from the same research group, which is an honest way of saying: this fits our existing hypothesis, but it’s also the same group building on its own prior work rather than an outside lab testing the claim independently.

A fourth paper worth mentioning briefly, since it turns up in the reference list, looked at organotypic pineal cell culture rather than cortical or cerebellar neurons. Khavinson, Linkova, Chalisova, and colleagues tested several bioregulator peptides on pinealocyte cultures from rat pineal glands and found that EDR did not affect the apoptosis marker AIF, unlike Epithalon’s dipeptide relative Lys-Glu-Asp, which showed different signaling effects entirely. It’s a useful negative-ish result: EDR isn’t doing everything all the bioregulator peptides do, which cuts against the idea that these compounds are interchangeable and supports the tissue-specificity part of Khavinson’s framework (PMID 22803060). A more recent 2020 paper in Molecules revisited the DNA interaction hypothesis specifically in the context of Alzheimer’s disease pathogenesis, proposing a mechanism by which EDR peptide binding to gene promoter regions could influence protein synthesis pathways relevant to neurodegeneration (PMID 33396470). That paper is theoretical and mechanism-focused rather than new experimental data, but it shows the group is still actively extending the framework a decade after the original nuclear-penetration work.

Put those together and you get a coherent, if narrow, story. A short peptide gets into the nucleus and binds DNA with some sequence preference (HeLa cells, in vitro). That same peptide shows gene expression linked effects in specific neuronal and pineal cell types (aging cortex cultures, organotypic pineal culture). It reduces oxidative stress markers and modulates cell cycle activity across three different cell types in a dose dependent way. And in a live rodent model of prenatal metabolic stress, maternal treatment correlates with reduced oxidative markers and better offspring outcomes. None of these papers has a large sample size by modern standards, and all of them trace back to overlapping author lists centered on Khavinson’s institute. The story holds together internally. It just hasn’t been tested by anyone outside that circle yet, as far as the published record shows.

Where the Evidence Base Is Limited

This is the part most Pinealon content skips, and it’s the part we think matters most. Nearly every citation you’ll find attached to Pinealon traces back to Vladimir Khavinson, either as sole author, senior author, or a close collaborator publishing with his institute. That’s not a minor caveat. It’s the single most important thing to understand before weighting any claim about this compound.

Why does single-source literature matter so much? Independent replication is how science self-corrects. When only one lab (or one closely connected research network) has ever produced a finding, there’s no external check on methodology, no second team stumbling onto a confound the original researchers missed, no failed replication attempt to flag a result that doesn’t hold up. That doesn’t mean the Khavinson group’s data is wrong. Plenty of legitimate, eventually-validated findings started life as a single lab’s result before anyone else picked it up. But it does mean the evidentiary weight sits lower than a comparable finding that’s been reproduced by two or three unconnected groups using different methods.

A second limitation: most of the CNS and neuroprotection data comes from cell culture and rodent studies, not from large, controlled trials in any species, human or otherwise. Rodent sample sizes in the papers we reviewed run small by contemporary standards. The prenatal hyperhomocysteinemia study, for instance, is exactly the kind of design where litter size and maternal variability introduce noise that a bigger cohort would average out. None of this is unusual for peptide bioregulator research broadly, but it does mean effect sizes reported in these papers should be read as preliminary signals, not confirmed magnitudes.

Third, publication venue matters and is worth naming directly. Several of the core Pinealon papers appeared in journals with a narrower international footprint and less rigorous peer review infrastructure than flagship Western journals in molecular biology or neuroscience. That’s not an accusation of fraud, and it doesn’t make the underlying chemistry wrong. It does mean the vetting process these papers went through before publication was, on average, less adversarial than what you’d expect from a paper submitted to, say, Cell or Nature Neuroscience.

Here’s why we think stating this plainly actually strengthens the case for taking the compound seriously as a research tool, rather than weakening it. A lot of peptide marketing content either ignores this limitation entirely or buries it in a single throwaway line. We’d rather researchers know exactly what they’re working with going in: a mechanistically interesting hypothesis, a small but internally consistent body of supporting data, and essentially zero independent replication outside the group that generated the original claims. That’s a specific, honest description of the evidence, and it’s more useful to a researcher deciding whether to design a follow-up experiment than a glowing summary that overstates certainty.

Nearly all published Pinealon research traces back to a single research network, a limitation worth stating plainly.

How Pinealon Compares to Related Compounds

Pinealon rarely gets studied in a vacuum, in the literature or in practice. Here’s how it stacks up against three compounds researchers most often ask about alongside it.

Semax. Semax is a heptapeptide derived from ACTH(4-10), developed separately in Russian neuropharmacology research and structurally unrelated to the Khavinson bioregulator family. Where Pinealon’s proposed mechanism runs through direct DNA interaction, Semax research centers on BDNF (brain-derived neurotrophic factor) expression and modulation of the dopaminergic and serotonergic systems. Researchers frequently examine the two side by side precisely because they’re mechanistically distinct but both framed around cognitive and CNS research applications. We go deeper on how Pinealon and Semax differ in cognitive research, including receptor targets and study design differences.

Epithalon. Easy to confuse with Pinealon by name alone, but the two occupy different spots in Khavinson’s framework. Epithalon (Ala-Glu-Asp-Gly, AEDG) is the pineal-gland-derived tetrapeptide most associated with telomerase activation research and circadian rhythm studies, while Pinealon is the CNS-broad tripeptide. Both share the same interpretive lens (short peptide, tissue-specific regulatory function, proposed epigenetic mechanism), which makes for a useful comparison when researchers are trying to understand the internal logic of Khavinson’s peptide bioregulator program as a whole. See our breakdown of how Epithalon and Pinealon compared for the full mechanistic side by side.

DSIP. Delta sleep-inducing peptide is a different animal again, a nonapeptide first isolated from rabbit brain in the 1970s and studied mainly for its association with slow-wave sleep architecture, independent of Khavinson’s group entirely. The comparison with Pinealon comes up in sleep and stress research contexts, where researchers sometimes look at both compounds as candidates for CNS modulation, even though their proposed mechanisms don’t overlap much. Our page on DSIP and Pinealon in sleep research covers where the two diverge and where a research design might reasonably include both.

For a broader look at how these mechanisms interact under stress conditions specifically, we also cover stress, sleep and cognitive research involving Pinealon and Semax in more depth, including how researchers have paired the two in stacked designs.

Stack Rationale: What Pairs With Pinealon and Why

If the working hypothesis is that Pinealon acts through gene expression modulation in CNS tissue, the logical research pairing is a compound with a different, non-overlapping mechanism, so any observed effect in a combined protocol can at least be partially attributed to one pathway or the other rather than two compounds doing the same thing redundantly. That’s the reasoning behind Spartan’s Cognitive Research Stack, which pairs Pinealon with Semax (BDNF and monoamine pathway research) and NAD+ (cellular energy metabolism research). Three distinct mechanistic angles on CNS and cognitive research, rather than three compounds competing for the same proposed effect.

Researchers focused specifically on the aging and longevity angle of the bioregulator hypothesis sometimes pair Pinealon with Epithalon instead, since both come from the same theoretical framework and the comparison itself, CNS-broad tripeptide against pineal-specific tetrapeptide, is often the research question. That pairing makes more sense for a study designed around Khavinson’s tissue-specificity hypothesis than for a general cognitive research protocol.

Pharmacokinetic Profile

Short peptides like Pinealon behave differently from larger therapeutic peptides in ways that matter for research handling. At three amino acids, EDR is small enough that some researchers have proposed it can cross the blood-brain barrier through passive diffusion, unlike larger peptides that typically need active transport mechanisms or specialized delivery routes to reach CNS tissue. Khavinson’s group has published radiolabeled distribution studies in rodents suggesting tissue patterns consistent with CNS penetration after systemic administration, though independent pharmacokinetic verification using more rigorous, modern tracer methods would meaningfully strengthen this claim.

Stability is the other side of the story, and it’s a real practical concern with any short peptide. Tripeptides are generally more vulnerable to enzymatic degradation by peptidases than larger, more structurally complex peptides, since there’s less steric protection around the peptide bonds and fewer secondary structure features to shield them. That translates directly into research handling requirements: once reconstituted, short peptides like Pinealon typically have a shorter usable window in solution than larger compounds, and they’re more sensitive to temperature fluctuations and repeated freeze-thaw cycling. In cell culture and in vitro binding work, this isn’t usually a major obstacle since experiments run on a defined timeline, but it does mean fresh reconstitution and careful storage discipline matter more here than for a bulkier, more stable peptide.

Handling and Storage for Laboratory Research

Pinealon ships as a lyophilized (freeze-dried) powder, which is the standard format for short peptides because it maximizes shelf stability prior to use. Unreconstituted, lyophilized Pinealon stored at minus 20 degrees Celsius or below, protected from light and moisture, maintains stability well over extended periods, consistent with general lyophilized peptide storage practice.

Once reconstituted with bacteriostatic water, the clock starts moving faster. Refrigerated at 2 to 8 degrees Celsius, reconstituted short peptide solutions are generally most reliable within the first few weeks, though researchers should always treat published stability windows as an upper bound, not a target, and account for the specific buffer, concentration, and handling conditions in their own protocol. Avoid repeated freeze-thaw cycling. If a research design calls for aliquoting doses ahead of time, single-use aliquots frozen immediately after reconstitution reduce degradation risk compared to drawing repeatedly from one working vial.

Getting reconstitution volumes and concentrations right matters more with a small tripeptide, where dosing precision errors have an outsized effect relative to the total peptide mass involved. For step-by-step guidance on reconstituting lyophilised research peptides, including bacteriostatic water ratios and concentration calculations, see our full reconstitution guide.

Safety and Endocrine Considerations

All of the data discussed in this guide comes from in vitro cell culture systems or animal models, and none of it establishes safety or efficacy in humans. Pinealon is not approved for any human therapeutic use, and none of the published research supports human application in any form. Researchers designing studies involving Pinealon should account for standard laboratory safety practice around peptide handling: appropriate personal protective equipment, correct storage and disposal procedures, and institutional review where applicable for any animal model work.

On the endocrine side, the published literature doesn’t report significant hormonal axis interactions for Pinealon specifically, unlike some other bioregulator peptides in Khavinson’s broader catalog that were designed around specific endocrine tissues. That said, absence of reported endocrine effects in a small published literature is not the same as a confirmed absence of effect; it simply reflects what has and hasn’t been tested and published so far. Researchers should treat any preclinical peptide, including this one, as requiring its own hazard assessment rather than assuming a clean safety profile because adverse findings haven’t been reported in a limited number of studies from one research group.

Frequently Asked Questions

What is Pinealon?
Pinealon is a synthetic tripeptide with the sequence glutamate, aspartate, arginine (EDR), developed within Vladimir Khavinson’s peptide bioregulator research program at the St. Petersburg Institute of Bioregulation and Gerontology. It’s studied for interactions with DNA and effects in central nervous system cell models. Available for laboratory research only.

Is Pinealon the same as Epithalon?
No. They’re both part of the same bioregulator peptide family and share a similar theoretical framework, but Epithalon (Ala-Glu-Asp-Gly) is a tetrapeptide associated with the pineal gland and telomerase research, while Pinealon (Glu-Asp-Arg) is a tripeptide associated with broader CNS tissue. The naming similarity is a common source of confusion.

What does the DNA interaction hypothesis actually claim?
It proposes that short peptides like EDR can enter a cell nucleus and bind specific DNA sequence motifs, functioning as gene expression modulators. Fedoreyeva et al. demonstrated nuclear penetration and sequence-preferential DNA binding in HeLa cells using fluorescence quenching assays (PMID 22117547). It remains a hypothesis rather than an established mechanism, with limited independent confirmation.

Has Pinealon been tested in animal models?
Yes. A 2012 study in the International Journal of Clinical and Experimental Medicine examined Pinealon administration to pregnant rats with diet-induced hyperhomocysteinemia and found reduced oxidative stress markers and improved spatial learning in offspring (PMID 22567179). This is one of a small number of published animal studies, all originating from the same research network.

Why does nearly all Pinealon research come from one group?
Vladimir Khavinson’s institute originated the peptide bioregulator concept and has published the large majority of papers on Pinealon and related compounds. Independent research groups outside that network have not extensively taken up the compound, which means the findings, while internally consistent, lack the external replication that would normally strengthen confidence in a mechanism.

How does Pinealon differ from Semax mechanistically?
Semax’s proposed mechanism centers on BDNF expression and monoaminergic system modulation, structurally unrelated to Khavinson’s bioregulator framework. Pinealon’s proposed mechanism runs through direct nuclear DNA interaction. They’re studied together often because researchers want mechanistically distinct compounds for combined cognitive research protocols, not because they share a pathway.

What’s the stability profile for reconstituted Pinealon?
As a tripeptide, Pinealon is generally more vulnerable to enzymatic degradation than larger peptides once in solution. Lyophilized powder stored frozen and protected from light maintains stability over extended periods. Reconstituted solutions should be refrigerated, used within a conservative timeframe, and not subjected to repeated freeze-thaw cycling.

Can Pinealon cross the blood-brain barrier?
Its small tripeptide size makes passive diffusion across the blood-brain barrier more plausible than for larger peptides. Khavinson’s group has published radiolabeled tissue distribution data in rodents consistent with CNS penetration after systemic administration, but independent pharmacokinetic verification remains limited.

Where can researchers source Pinealon?
Spartan Peptides supplies Pinealon (EDR) for laboratory and in vitro research use. It’s also available as part of the Cognitive Research Stack alongside Semax and NAD+ for researchers designing multi-target CNS protocols. Not for human consumption or therapeutic use.

References

1. 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 (Mosc). 2011 Nov;76(11):1210-9. PMID: 22117547.
2. Khavinson V, Ribakova Y, Kulebiakin K, Vladychenskaya E, Kozina L, Arutjunyan A, Boldyrev A. Pinealon increases cell viability by suppression of free radical levels and activating proliferative processes. Rejuvenation Res. 2011 Oct;14(5):535-41. PMID: 21978084.
3. Arutjunyan A, Kozina L, Stvolinskiy S, Bulygina Y, Mashkina A, Khavinson V. Pinealon protects the rat offspring from prenatal hyperhomocysteinemia. Int J Clin Exp Med. 2012;5(2):179-85. PMID: 22567179.
4. Khavinson VKh, Lin’kova NS, Tarnovskaya SI, Umnov RS, Elashkina EV, Durnova AO. Short peptides stimulate serotonin expression in cells of brain cortex. Bull Exp Biol Med. 2014 May;157(1):77-80. PMID: 24909721.
5. Khavinson VKh, Linkova NS, Chalisova NI, Dudkov AV, Koncevaya EA. Effect of short peptides on expression of signaling molecules in organotypic pineal cell culture. Bull Exp Biol Med. 2011 Nov;152(1):138-41. PMID: 22803060.
6. 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. 2020;26(1):159. PMID: 33396470.