SNAP-8 Research, Specifications & Scientific Information

Introduction

SNAP-8 is a trade name. The substance behind it is acetyl octapeptide-3, an eight-residue synthetic peptide sold as a cosmetic ingredient, and the most important thing this page can report about it is what is missing.

No indexed study examines the isolated peptide. Searches of PubMed under each of its names return no primary research report on acetyl octapeptide-3 alone, and no study of it is registered on ClinicalTrials.gov. Where it appears in the peer-reviewed literature, it appears as one listed component of a multi-ingredient product alongside several other actives ^{[1, 2]}.

That is not an unusual position for a cosmetic ingredient. Cosmetic ingredients are not required to demonstrate efficacy before sale in the United States, so there is no regulatory mechanism that would generate the studies a medicine accumulates. The consequence for a reference page is straightforward: this one is short, it says what the identifiers are, it states the proposed mechanism as a hypothesis, and it is explicit that the studies it cites are about other things.

What Is SNAP-8?

SNAP-8 is the synthetic octapeptide Ac-Glu-Glu-Met-Gln-Arg-Arg-Ala-Asp-NH2, acetylated at the N-terminus and amidated at the C-terminus. Its International Nomenclature of Cosmetic Ingredients name is acetyl octapeptide-3; it also appears as acetyl glutamyl heptapeptide-3 and as acetyl octapeptide-1.

PubChem carries it under compound identifier 76283482, with CAS registry number 868844-74-0 and FDA/NCATS UNII code 8K14HJF88S.

Its sequence corresponds to a region of SNAP-25, the synaptosomal-associated protein that forms one arm of the SNARE complex — the machinery by which vesicles fuse with the plasma membrane during regulated exocytosis. That correspondence is the origin of the compound's design, and it is the whole of the rationale offered for it.

It is not a medicine in any jurisdiction. It has not been approved by the U.S. Food and Drug Administration for any indication, and no marketing application for it is on record in the United States.

SNAP-8 Specifications

SNAP-8 is a trade name; the International Nomenclature of Cosmetic Ingredients name for the substance is acetyl octapeptide-3, and it also appears as acetyl glutamyl heptapeptide-3 and acetyl octapeptide-1. PubChem carries it under compound identifier 76283482 with CAS registry number 868844-74-0 and the FDA/NCATS UNII code 8K14HJF88S. A second PubChem record, 71587832, appears under the same trade name and the same UNII but with a different molecular formula; the record cited here is the one carrying the CAS registry number and a composition consistent with the stated sequence, and the discrepancy is noted rather than resolved. The peptide is blocked at both ends — acetylated at the N-terminus and amidated at the C-terminus — and its sequence corresponds to the N-terminal region of SNAP-25, the synaptosomal-associated protein that forms part of the SNARE complex. The single methionine is an oxidation liability adding sixteen daltons when it forms the sulphoxide.

Values that a public register does not carry are shown as not publicly characterised rather than estimated. Identifiers are reference values; the certificate of analysis supplied with a laboratory order is the record for a given lot.

How Does SNAP-8 Work?

Nothing is established, and nothing has been tested in print.

The proposed mechanism is competitive interference with SNARE complex assembly. SNAP-25 contributes to that complex through defined regions of its sequence; a short peptide resembling one of those regions might, in principle, compete with the native protein during assembly and reduce the efficiency of vesicle fusion. That is the design premise, and it is the same premise as for the shorter peptide this one was patterned after.

Three things should be said about it plainly.

It is a hypothesis about a mechanism, not a measurement of one. No published experiment testing SNARE interference by acetyl octapeptide-3 was located for this page — no competition assay, no binding measurement, no cellular exocytosis endpoint.

A sequence resemblance is not a demonstrated interaction. Short peptides derived from the surfaces of large proteins frequently fail to reproduce the parent's binding, because the isolated segment lacks the conformational constraint the rest of the protein provides.

Delivery is a separate unanswered question. An eight-residue, highly charged, doubly blocked peptide has to reach an intracellular protein complex for the proposed mechanism to operate. Nothing published addresses whether it does.

SNAP-8 Mechanism of Action

No mechanistic study of this peptide exists in the indexed literature — no in vitro characterisation, no cell-based assay, no animal work. This page therefore states no mechanism as established, and the specification table records the target, receptor family and agonist status as not publicly characterised rather than filling them from a marketing description.

That is the accurate entry. The alternative — restating the SNARE hypothesis in the grammar of a finding — would convert a design premise into a claim, which is the failure this library is built to avoid.

What Is SNAP-8 Being Researched For?

Nothing, as an isolated compound. It has no research programme of its own.

Where it appears in the peer-reviewed record, it appears as an ingredient:

• A dissolving microneedle patch whose stated composition was a hyaluronic acid polymer backbone together with acetyl octapeptide-3, L-ascorbic acid 2-glucoside and further agents ^[1].
• A hyaluronic acid microneedle patch containing a polypeptide, acetyl octapeptide-3, palmitoyl tripeptide-5 and adenosine ^[2].

In both cases the peptide is one of several active components of a delivery system, and the studies were designed to evaluate the product rather than to isolate the contribution of any ingredient.

Human Research on SNAP-8

Human clinical research

Results from pharmaceutical clinical trials describe the investigational material and populations used in those studies and should not be interpreted as establishing the effects of research-grade materials offered for laboratory use.

What the two indexed human studies are

Dissolving microneedle patch, 2024. A clinical safety and efficacy evaluation of a dissolving microneedle patch whose stated composition includes a hyaluronic acid polymer backbone, acetyl octapeptide-3, L-ascorbic acid 2-glucoside and further agents ^[1].

Hyaluronic acid microneedle patch, 2020. A monocentric clinical study of bioactive peptides loaded on hyaluronic acid microneedle patches, the listed contents including a polypeptide, acetyl octapeptide-3, palmitoyl tripeptide-5 and adenosine ^[2].

Why no result from either is reported on this page

Both studies evaluated a finished multi-ingredient product delivered through a microneedle system. Whatever each measured, the measurement belongs to the combination of a delivery device and several actives. Attributing any portion of it to one listed ingredient would require a design that isolates that ingredient — a comparison against the same patch without it, at minimum — and neither study was built that way.

Reporting a number from those papers under this compound's name would therefore be a misattribution, and this page does not do it. The studies are cited so that a reader can see exactly what the indexed literature contains.

The related hexapeptide

What exists for it. Acetyl hexapeptide-8, marketed as Argireline, is the shorter peptide this one was patterned after, and it does have direct clinical literature: a randomised, placebo-controlled study in Chinese subjects ^[3] and a separate efficacy report ^[4].

What that means here. It means the field is capable of producing controlled studies of an individual peptide of this class, and that none has been produced for this one. Those studies were conducted with a different molecule of a different length, and their results are not transferable. They are cited to mark the boundary, not to cross it.

Current Research Status

Status as of September 22, 2026. This block is rendered from maintained fields, not from prose, so it cannot go stale in one place and stay current in another.

SNAP-8 vs Related Compounds

Against Argireline

Acetyl hexapeptide-8 is six residues; this peptide is eight. Both are patterned on SNAP-25 sequence and both are sold as cosmetic ingredients. The hexapeptide has randomised placebo-controlled clinical literature of its own ^[3]; this one has none. Where two closely related ingredients differ in that way, the difference is the most useful fact about them.

Against botulinum toxin

The SNARE rationale invites the comparison, since botulinum neurotoxin acts by proteolytically cleaving SNAP-25. The comparison is worth stating only to dismiss it: an enzyme that irreversibly cuts a protein and a short peptide that may or may not compete with it during assembly are not mechanistically comparable, and no published evidence places this peptide in that category.

Against the peptides in this library with their own literature

GHK-Cu and KPV are also short peptides studied in skin-related contexts, and both have primary research records examining the isolated molecule. That is the ordinary situation for a compound with an entry here, and it is the situation this one is not in.

What would change the picture

A single controlled study of the isolated peptide — a binding or competition assay for the SNARE claim, or a clinical comparison against an otherwise identical vehicle — would move this compound from an ingredient with a rationale to an ingredient with evidence.

No comparison of effect between these compounds is made on this page.

Chemical & Molecular Characteristics

SNAP-8 is an eight-residue peptide of molecular formula C41H70N16O16S and average mass 1075.2 g/mol, under PubChem compound identifier 76283482 and CAS registry number 868844-74-0.

Two register records, one substance, a discrepancy worth knowing about. A second PubChem record, 71587832, appears under the same trade name and the same UNII but carries a different molecular formula. This page cites the record that carries the CAS registry number and a composition consistent with the stated sequence. The discrepancy is noted rather than resolved, because resolving it would require correcting a public register rather than reading one.

Both termini are blocked. Acetylation at the N-terminus and amidation at the C-terminus remove the charges that exopeptidases and ion-exchange methods use. Both are intended stability features, and the C-terminal amide is one dalton from the free acid — a difference that routine intact-mass measurement on a 1075-dalton peptide will not reliably resolve.

One methionine, which oxidises. The methionine at position 3 forms the sulphoxide readily, adding sixteen daltons and producing a species chromatographically distinct from the parent but often incompletely resolved from it. In an eight-residue peptide this is the dominant degradation route and the one a certificate of analysis should address.

Strongly charged, in both directions. Two glutamates and an aspartate against two arginines give the molecule a substantial and opposed charge distribution across a very short backbone. This affects solubility, chromatographic retention and — relevant to the proposed mechanism — any prospect of crossing a membrane unaided.

No aromatic residue. There is no tryptophan, tyrosine or phenylalanine, so absorbance at 280 nm is negligible and quantification must rely on peptide-bond absorbance near 214 nm or on an alternative method.

Frequently Asked Questions

Scientific References

1. Shin JY, Han D, Yoon KY, et al.. Clinical Safety and Efficacy Evaluation of a Dissolving Microneedle Patch Having Dual Anti-Wrinkle Effects With Safe and Long-Term Activities Annals of dermatology; 2024. PMID 39082657 doi:10.5021/ad.23.136
2. Avcil M, Akman G, Klokkers J, et al.. Efficacy of bioactive peptides loaded on hyaluronic acid microneedle patches: A monocentric clinical study Journal of cosmetic dermatology; 2020. PMID 31134751 doi:10.1111/jocd.13009
3. Wang Y, Wang M, Xiao S, et al.. The anti-wrinkle efficacy of argireline, a synthetic hexapeptide, in Chinese subjects: a randomized, placebo-controlled study American journal of clinical dermatology; 2013. PMID 23417317 doi:10.1007/s40257-013-0009-9
4. Wang Y, Wang M, Xiao XS, et al.. The anti-wrinkle efficacy of Argireline Journal of cosmetic and laser therapy : official publication of the European Society for Laser Dermatology; 2013. PMID 23464592 doi:10.3109/14764172.2013.769273

Every identifier above is resolved against PubMed, Crossref or ClinicalTrials.gov at build time, and the title returned by the register is compared with the title stored here. A page does not publish if a reference fails to resolve.

Research-Use Information

For in vitro research use only. This material is a laboratory reagent. It is not a drug, food, dietary supplement, or cosmetic and is not for human or veterinary use, including ingestion, injection, or any other administration. No information on this page describes or implies any effect in humans or animals. Sold only to researchers under our Terms of Sale.