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Peptide Research Library

SNAP-8

the SNARE-mimicking expression-line peptide
Acetyl Octapeptide-3; Acetyl Glutamyl Heptapeptide-1; Ac-EEMQRRAD-NH₂
For research use only Evidence grade C — in-vitro mechanism + manufacturer cosmetic testing Cosmetic / Skin

SNAP-8 is a synthetic acetylated octapeptide (INCI Acetyl Octapeptide-3, also listed as Acetyl Glutamyl Heptapeptide-1) marketed as a topical cosmetic active for the appearance of expression lines. It is an elongated analog of Acetyl Hexapeptide-8 (Argireline), originally developed by Lipotec, and is reported to mimic the N-terminal domain of the SNAP-25 protein.13 It is a cosmetic ingredient and laboratory reference material, not an approved drug; published evidence is limited to in-vitro/cell SNARE studies and manufacturer-conducted cosmetic testing rather than peer-reviewed clinical trials.12 Multiple molecular descriptors circulate in the literature, so the values below are derived from the verified amino-acid sequence and cross-checked against PubChem.4

Structure

Sequence & identity

AcGluGluMetGlnArgArgAlaAspNH₂
Ac-Glu-Glu-Met-Gln-Arg-Arg-Ala-Asp-NH₂ · C₄₁H₇₀N₁₆O₁₆S · 1075.16 g/mol

Structure and identity per PubChem CID 76283482 (InChIKey KMACPCJUCHVVGP-FNRPHRCSSA-N), the C-terminally amidated octapeptide (Ac-…-Asp-NH₂), consistent with supplier specifications for Acetyl Octapeptide-3.4

What the research shows

Mechanisms studied

Researchers describe SNAP-8 as a competitive mimic of the N-terminal end of SNAP-25, a component of the SNARE complex that mediates calcium-dependent fusion of neurotransmitter vesicles at the neuromuscular junction.3 The conceptual basis traces to studies in which synthetic peptides corresponding to SNAP-25 sequences inhibited regulated exocytosis: Gutiérrez and colleagues reported that a SNAP-25 C-terminal peptide blocked the slow, ATP-dependent docking step of catecholamine secretion in bovine chromaffin cells, causing accumulation of docked dense-core vesicles.1 By analogy, SNAP-8 is proposed to destabilize SNARE assembly and thereby attenuate stimulated catecholamine/acetylcholine release; direct mechanistic data specific to the SNAP-8 octapeptide itself remain limited.13

Reported in studies

Dosing in the research literature

The figures below summarise regimens as reported in published research — they are not recommendations or directions for use.

Source / modelRegimen reportedNotes
r2Topical cosmetic emulsions formulated at roughly 3–10% of the supplier’s peptide solution (which is itself a dilute active concentrate), applied to expression-line areas in manufacturer testing.Reported as used in cosmetic formulation/manufacturer studies, not a clinical dosing protocol. RUO material is not for human application; no established therapeutic dose exists.
r1In-vitro chromaffin-cell exocytosis assays used micromolar SNAP-25-derived peptide concentrations introduced intracellularly.Cell-model concentrations only; not translatable to topical or systemic human dosing.
Research use only. Peptigo products are sold to qualified researchers for laboratory use. This information summarises published research for reference and is not medical advice, a dosing recommendation, or directions for human or animal use.
Reported in studies

Effects observed in research

In bovine chromaffin-cell models, SNAP-25-derived peptides were observed to inhibit the ATP-dependent docking component of regulated secretion, reducing stimulated catecholamine release.1 For the SNAP-8 octapeptide specifically, the manufacturer (Lipotec) reported in its own in-vivo cosmetic testing a reduction in periorbital wrinkle depth (figures around a ~63% relative reduction) over 28 days of twice-daily topical use of a 10% formulation versus vehicle; these figures derive from company technical literature rather than independent peer-reviewed trials and should be read with that caveat.23 Suppliers describe topical use as well tolerated with no systemic neuromuscular effects reported, a claim consistent with the limited skin penetration expected of a hydrophilic charged peptide but one for which rigorous independent safety and efficacy data are sparse.3

Honest assessment

Strength of evidence

Grade C

Grade C. The mechanistic rationale rests on in-vitro and cell-based SNARE/SNAP-25 exocytosis studies1 rather than studies of SNAP-8 in humans. Anti-wrinkle efficacy claims originate largely from manufacturer-conducted cosmetic testing and trade literature, not randomized controlled trials, and independent replication is limited.23 Analytical characterization (e.g., LC-MS/MS quantification methods) has been published.5 No reliable human pharmacokinetic half-life for topical SNAP-8 has been established. SNAP-8 is a cosmetic ingredient / research reagent and is not an approved therapeutic drug.

Handling

Reconstitution & storage

Reconstitute with bacteriostatic water for laboratory handling. Store lyophilised material frozen and reconstituted material refrigerated. Use Peptigo’s reconstitution calculator and storage cheat sheet for working figures.

References

References

  1. Gutiérrez LM, Viniegra S, Rueda J, Ferrer-Montiel AV, Canaves JM, Montal M. A peptide that mimics the C-terminal sequence of SNAP-25 inhibits secretory vesicle docking in chromaffin cells. J Biol Chem. 1997 Jan 31;272(5):2634-2639. PMID: 9006897.
  2. Lipotec S.A.U. SNAP-8 (Acetyl Glutamyl Heptapeptide-1) technical/marketing documentation, including in-vivo anti-wrinkle test data. Manufacturer literature (UL Prospector / Lotioncrafter product listings). https://www.ulprospector.com/en/na/PersonalCare/Detail/2670/81055/SNAP-8-peptide-solution-C
  3. INCI / cosmetic ingredient profile: Acetyl Octapeptide-3 (SpecialChem cosmetics ingredient database; supplier monographs describing SNAP-25 / SNARE mimicry mechanism). https://www.specialchem.com/cosmetics/inci-ingredients/acetyl-octapeptide-3
  4. PubChem Compound Summary for CID 76283482, Acetyl octapeptide-3 / SNAP-8 (molecular formula C41H70N16O16S; InChIKey KMACPCJUCHVVGP-FNRPHRCSSA-N; CAS 868844-74-0). National Library of Medicine. https://pubchem.ncbi.nlm.nih.gov/compound/76283482
  5. Method development for acetyl octapeptide-3 analysis by liquid chromatography–tandem mass spectrometry. Journal of Analytical Science and Technology. 2020;11:38. https://doi.org/10.1186/s40543-020-00232-8