Published · 11 references

Epitalon vs Pinealon

Epitalon and Pinealon are not the same molecule: Epitalon is a synthetic four-residue peptide, and Pinealon is a synthetic three-residue peptide.

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Structure at a glance

Each chain as stored in the product database, one box per residue. The two are drawn separately; no alignment between them is implied.

Epitalon · 4 residues

Pinealon · 3 residues

Letters are one-letter amino acid codes.

Chain length
Epitalon4 residues
Pinealon3 residues
Molecular weight
Epitalon390.35 g/mol
Pinealon418.41 g/mol

Drawn from the product database. Each measure's bars share one scale.

Epitalon vs Pinealon, compared
What it isA four-residue peptide, designed from the amino acid composition of Epithalamin, a bovine pineal gland extract.[1] Also written Epithalon.A three-residue peptide. Despite its name, not a pineal gland extract.
How they relateDifferent molecules. Epitalon was designed from the amino acid composition of Epithalamin, a bovine pineal gland extract.[1] Pinealon is a synthetic three-residue peptide. Both belong to one research program's synthetic peptide series.
CAS number307297-39-8175175-23-2
Molecular formulaC14H22N4O9C15H26N6O8
Molecular weight390.35 g/mol418.41 g/mol
SequenceAEDGEDR
TargetNo target established for Epitalon. Binding to DNA at gene promoters is a proposal, not a demonstrated mechanism.No target established for Pinealon.
Evidence baseFDA's literature search found three human studies.[2] The strongest of them did not specify blinding.[2] Also animal and in vitro studies. One research group produced almost all of the literature.Three human reports. None is randomized, controlled, blinded or registered.[3] Also animal and in vitro studies. One research group produced almost all of the literature.
Regulatory statusThe FDA has not approved Epitalon for human use. A US orphan drug designation was granted in 2010 and withdrawn or revoked in 2016.[2] Designation is not approval.The FDA has not approved Pinealon for human use.
Compared head-to-head?Yes: a 2008 report tested Epitalon, Pinealon and two other short peptides, each in its own group, in vitro.[4] A second 2008 report tested the same four peptides in a rat model.[5] Further comparisons found in PubMed (searched October 2026).[6]
Handling differenceNeither contains a cysteine, a methionine or an aromatic residue. Epitalon's aspartate is followed by glycine, the classic succinimide-forming pair. Pinealon's N-terminal glutamate can cyclize to pyroglutamate, and its aspartate can rearrange, more slowly.

How Epitalon and Pinealon differ

Epitalon and Pinealon are not the same molecule. Epitalon is a synthetic tetrapeptide, a chain of four amino acids, and Pinealon is a synthetic tripeptide, a chain of three. Both belong to the synthetic series of very short peptides developed by one research program.

Epitalon was designed from the amino acid composition of Epithalamin, a bovine pineal gland extract.[1] Epithalamin is an undefined mixture of animal tissue, and a result obtained with it is not a result for Epitalon. Despite its name, Pinealon is not a pineal gland extract.

FDA's literature search found three human studies of Epitalon.[2] The strongest of them did not specify blinding.[2] Pinealon's human record is three reports. None is randomized, controlled, blinded or registered.[3]

One research group produced almost all of the literature on each compound: the group that discovered these peptides. Across the series, independent replication in other laboratories has been limited. The proposed binding to particular stretches of DNA is not a broadly validated mechanism in mainstream molecular biology.

In this series, the one experimental NMR study of peptide-DNA binding used Pinealon's three-residue sequence, not Epitalon.[7] That 2019 study examined the tripeptide with DNA in solution, without cells.[7] The research program's leader is not an author of that study, but its senior author has co-authored with him before. In the literature reviewed for Pinealon, that study should not be over-read.[3] Across the series, there is still no deposited structure and no dissociation constant.[3]

Have Epitalon and Pinealon been compared directly?

A 2008 report tested Epitalon, Pinealon and two other short peptides, each in its own group, in vitro on human lipoproteins, red blood cells and cultured neurons.[4] A second 2008 report tested the same four peptides in a rat hypobaric hypoxia model, and its abstract does not name the measure.[5] A 2011 study tested fluorescently tagged forms of both, among other short peptides, in cultured HeLa cells, a human cell line.[8] Another 2011 study tested both, among four short peptides, in organotypic cultures of rat pineal gland.[9] A 2013 cell-free assay tested both, among six short peptides, against fluorescently labeled wheat histones.[10] A 2024 study tested both, among three short peptides, on human neurons induced from skin fibroblasts of older adult donors.[11] All of these papers come from the developer's research group and its collaborators. Results are reported for each compound in each paper.

Read more on each compound

Frequently Asked Questions

Is Epitalon the same as Pinealon?+

Epitalon and Pinealon are different molecules: Epitalon is a synthetic four-residue peptide, and Pinealon is a synthetic three-residue peptide. Both belong to the synthetic series developed by one research program. Epitalon was designed from the amino acid composition of Epithalamin, a bovine pineal gland extract. Despite its name, Pinealon is not a pineal gland extract.

References

  1. 1
    Araj SK, Brzezik J, Madra-Gackowska K, Szeleszczuk L. International Journal of Molecular Sciences. 2025;26(6):2691. PMID 40141333.
  2. 2
    US Food and Drug Administration, Center for Drug Evaluation and Research. Briefing Document, Pharmacy Compounding Advisory Committee, July 2026. fda.gov
  3. 3
    PubMed E-utilities corpus and absence searches, and ClinicalTrials.gov API v2 query, run 27 August 2026. (Family names and sequence codes crossed with NMR return only PMID 30762356 plus one unrelated receptor-modeling record; no deposited structure, Kd, SELEX motif or ChIP occupancy located across the family; no registered trial for pinealon.)
  4. 4
    Kozina LS, Arutiunian AV, Stvolinskii SL, Khavinson VKh. [Biological activity of regulatory peptides in model experiments in vitro]. 2008;21(1):68-73. PMID 18546826.
  5. 5
    Kozina LS. 2008;21(1):61-67. PMID 18546825.
  6. 6
    PubMed search via NCBI E-utilities, run 3 October 2026; records entered to 2 October 2026. Query: ("epitalon"[tiab] OR "epithalon"[tiab] OR "epithalone"[tiab] OR "AEDG"[tiab] OR "Ala-Glu-Asp-Gly"[tiab]) AND ("pinealon"[tiab] OR "Glu-Asp-Arg"[tiab] OR "EDR"[tiab]) AND ("1800/01/01"[edat] : "2026/10/02"[edat]). 11 records, including the 6 comparisons described above.
  7. 7
    Silanteva IA, et al. Journal of Physical Chemistry B. 2019;123(9):1896-1902. doi:10.1021/acs.jpcb.8b10359. PMID 30762356
  8. 8
    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;76(11):1210-1219. PMID 22117547
  9. 9
    Khavinson VKh, Linkova NS, Chalisova NI, Dudkov AV, Koncevaya EA. Effect of short peptides on expression of signaling molecules in organotypic pineal cell culture. Bulletin of Experimental Biology and Medicine. 2011;152(1):138-141. PMID 22803060.
  10. 10
    Fedoreyeva LI, et al. Biochemistry (Moscow). 2013;78(2):166-175. PMID 23581987.
  11. 11
    Kraskovskaya N, Linkova N, Sakhenberg E, Krieger D, Polyakova V, Medvedev D, Krasichkov A, Khotin M, Ryzhak G. International Journal of Molecular Sciences. 2024;25(21):11363. PMID 39518916.
Comparison

Epitalon vs N-Acetyl Epitalon

N-Acetyl Epitalon is a chemically modified form of Epitalon: the same four residues, with an N-terminal acetyl group and a C-terminal amide.

Read Comparison

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