SNAP-8

Technical data

CAS

868844-74-0

Molecular formula

C42H72N16O15S

Molecular weight

1075.16 g/mol

Identity and composition

SNAP-8 (Acetyl Octapeptide-3, also called Acetyl Glutamyl Heptapeptide-1) is a synthetic octapeptide studied as a smoothing agent for topically applied expression lines. It belongs to the class of SNARE-complex-modulating peptides derived from SNAP-25. Product for research use.

As for its chemical identity, the confirmed molecular formula is C42H72N16O15S, with an approximate molecular weight of 1073.2 g/mol (calculated from the formula registered in PubChem CID 71587832). It is described as an N-acetylated and amidated octapeptide, with a consensus sequence Ac-Glu-Glu-Met-Gln-Arg-Arg-Ala-Asp-NH2 (Ac-EEMQRRAD-NH2), consistent with the confirmed formula.

The CAS number is not included because it was not possible to confirm it in primary reference sources (the values circulating in catalogs appear with inconsistent names), so it is omitted rather than reporting an unverified datum.

Among its synonyms are: SNAP-8, Acetyl Octapeptide-3, Acetyl Glutamyl Heptapeptide-1 and Acetyl-EEMQRRAD-amide.

Mechanism of action

SNAP-8 was designed as a mimic of the N-terminal end of the SNAP-25, one of the proteins of the complex SNARE which mediates the fusion of synaptic vesicles and the release of neurotransmitters (including acetylcholine) at the neuromuscular junction.

The proposed mechanism for this class of peptides is the competition with native SNAP-25 for its incorporation into the SNARE complex, interfering with the assembly and stability of the complex and thus reducing calcium-dependent exocytosis (mechanism described for the parent peptide Argireline; Blanes-Mira et al., Int J Cosmet Sci 2002, PMID 18498523). SNAP-8 is a two-amino-acid extension (Ala-Asp) of Argireline (acetyl hexapeptide-3, Ac-EEMQRR-NH2), so it shares this proposed mechanism of action.

Unlike botulinum toxin, which irreversibly cleaves SNAP-25 enzymatically, the peptide inhibition of this class is described as non-covalent, competitive and reversible.

Pharmacokinetics

No peer-reviewed human pharmacokinetics were found for SNAP-8 in primary sources, so it is not possible to report values for half-life, absorption, or distribution.

Qualitatively, being a relatively large hydrophilic peptide (molecular weight close to 1073 Da), its transdermal penetration is limited; this point is discussed in the cosmetic literature but is not quantified in verifiable primary sources. Any quantitative characterization would fall outside what the available evidence supports.

Scientific evidence

The available evidence on SNAP-8 should be considered preliminary and limited in scope. It is a peptide for cosmetic/topical use and not a drug in regulated clinical development: no ClinicalTrials.gov records specific to SNAP-8 or phase I–III pharmacological trials were identified.

Most of the efficacy data comes from short cosmetic studies and secondary sources, several funded by the manufacturer of the material, so the wrinkle-reduction figures in circulation have not been independently verified and are not reproduced here. The mechanistic basis of the class (interference with the SNARE complex) is documented in vitro for the parent peptide Argireline (Blanes-Mira et al., Int J Cosmet Sci 2002, PMID 18498523), not directly for SNAP-8.

Overall, the preliminary evidence suggests research interest around the topical smoothing of expression lines, but without solid, independent clinical data that would allow affirming effect magnitudes.

Research applications

Product for research use. The following framing describes research contexts only.

It may be of interest for research in:

• In vitro studies on SNARE-complex-modulating peptides derived from SNAP-25.
• Comparative work within the family of topical "Botox-type" peptides (hexapeptides and pentapeptides that modulate neurotransmission).
• Physicochemical and laboratory-handling characterization of acetylated and amidated octapeptides.

Not applicable for:

• clinical use, ingestion or any clinical or therapeutic use.
• Injectable or systemic use: there is no published, peer-reviewed systemic toxicological evaluation supporting those routes.
• Any application involving diagnosis, treatment, or prevention of health conditions.

Research protocols

There are no validated pharmacological dosing protocols for SNAP-8. The literature identified corresponds to short-duration topical cosmetic studies and to secondary sources, without reproducible dose regimens in a peer-reviewed primary source, so no specific study quantities are reported to avoid carrying over unverified figures.

The research presentation format corresponds to a lyophilized vial of 10 mg. The definition of working concentrations and reconstitution volumes is left to the discretion of each laboratory's experimental design, within a strictly research framework.

Reconstitution

As a general laboratory handling guide for a lyophilized vial, peptide reconstitution is usually carried out with bacteriostatic water (sterile water with approximately 0.9% benzyl alcohol), which helps limit microbial growth in preparations intended for prolonged handling.

Suggested general steps:

• Let the vial reach room temperature before opening it.
• Add the diluent, letting it run slowly down the inner wall of the vial, without directing the stream straight onto the powder.
• Do not shake vigorously; swirl the vial gently until complete dissolution.
• The diluent volume defines the final concentration and is chosen according to the experimental design.

This technique is general laboratory knowledge and does not imply an indication for use in humans.

Stability and storage

As a laboratory handling standard for this class of peptides:

• Lyophilized (unreconstituted): the dry powder is the most stable form. It is usually stored refrigerated or frozen and protected from moisture and light; in freezing, long-term stability is greater.
• Reconstituted: once in solution, stability decreases and it is advisable to keep it refrigerated, use it within a short period, and avoid repeated freeze-thaw cycles.

These are general qualitative peptide-storage guidelines; there are no specific peer-reviewed stability data available for SNAP-8.

Safety profile

No safety notes from regulatory or solid primary sources were found for SNAP-8. The topical cosmetic studies cited in secondary sources describe good local tolerability, but there is no published, peer-reviewed systemic toxicological evaluation for injectable or systemic use.

Consequently, there are no safety data supporting the routes of administration implied by a 10 mg research vial, nor contraindications formally documented in primary sources. This data gap should be interpreted as an important limitation: the absence of reports of adverse events is not equivalent to an established safety profile.

For responsible laboratory handling, it is recommended to treat it as a research material with an uncharacterized profile, with the usual handling precautions (protective equipment, avoid contact and inhalation) and restricted to trained personnel.

Comparative context

SNAP-8 is grouped within the SNARE complex-inhibiting peptides derived from SNAP-25.

• Compared to Argireline (acetyl hexapeptide-3, Ac-EEMQRR-NH2): SNAP-8 is a two-amino-acid extension (Ala-Asp) of that parent sequence. Some secondary sources suggest a greater relative activity than that of Argireline, but this is not confirmed in a primary source, so it is presented only as an unverified observation.
• Compared to other topical "Botox-like" peptides (for example, pentapeptides and hexapeptides that modulate neurotransmission): they share a proposed reversible and competitive mechanism on the assembly of the SNARE complex.
• Compared to botulinum toxin: the key contrast is the type of action. The toxin acts enzymatically and irreversibly on SNAP-25, whereas the peptidic inhibition of this class is described as non-covalent, competitive, and reversible.

History and development

SNAP-8 emerges as an evolution within the family of cosmetic peptides that modulate the SNARE complex. Its conceptual starting point is Argireline (acetyl hexapeptide-3), a peptide that mimics the N-terminal end of SNAP-25 developed for the smoothing of expression lines; the mechanistic characterization of that parent peptide was described by Blanes-Mira et al. in Int J Cosmet Sci (2002, PMID 18498523).

SNAP-8 is constructed by extending the Argireline sequence with two additional amino acids (Ala-Asp), and it was marketed as a topical anti-wrinkle ingredient, associated in the secondary literature with the material's manufacturer (Lipotec). Unlike compounds with regulated clinical development, SNAP-8 does not have a formal program of pharmacological trials; its trajectory lies in the cosmetic/topical and materials research field.

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