SNAP-8 Peptide: Research Guide (Acetyl Octapeptide-3)
By UK Peptide Lab Research Team•19 September 2026•7 min read
Key Takeaways
- SNAP-8 is the acetyl octapeptide Ac-Glu-Glu-Met-Gln-Arg-Arg-Ala-Asp-NH₂, molecular weight approximately 1075 g/mol, CAS 868844-74-0, designed as an extension of acetyl hexapeptide-3 (Argireline).
- Both peptides mimic the N-terminal region of SNAP-25, the SNARE complex protein cleaved by botulinum neurotoxin A. Blanes-Mira et al. (J Neurochem, 2004) reported that N-terminal peptides inhibit SNARE complex formation and calcium-dependent catecholamine exocytosis in chromaffin cells.
- The cosmetic evidence is thinner than most summaries admit: the published 30% wrinkle-depth figure belongs to the hexapeptide's small open-label volunteer study (Blanes-Mira et al., Int J Cosmet Sci, 2002), and SNAP-8's own efficacy figures are largely manufacturer dossier material.
- SNAP-8 holds no marketing authorisation anywhere and is supplied for in-vitro laboratory research only, with no dosing information and no human-use claims.
What is SNAP-8?
SNAP-8, catalogued as acetyl octapeptide-3, is a synthetic eight-residue peptide with the sequence Ac-Glu-Glu-Met-Gln-Arg-Arg-Ala-Asp-NH₂, written Ac-EEMQRRAD-NH₂ in one-letter code. It carries an acetyl group at the N-terminus and a carboxamide at the C-terminus, has the molecular formula C₄₁H₇₀N₁₆O₁₆S, a molecular weight of approximately 1075 g/mol and CAS number 868844-74-0. The peptide was designed by the peptide chemistry group behind acetyl hexapeptide-3 (Argireline) as a deliberately extended version of that hexapeptide, adding an alanine and an aspartate at the C-terminus, and it was developed and marketed for cosmetic science by Lipotec. Three arginine residues give the sequence a strong positive charge and make it freely water soluble. UK Peptide Lab supplies SNAP-8 10mg as lyophilised powder for in-vitro laboratory research only.
SNAP-25 and the SNARE Complex
To understand SNAP-8 you have to start with SNAP-25, the synaptosome-associated protein of 25 kDa that the peptide mimics. At the presynaptic terminal, vesicle fusion is driven by a four-helix bundle called the SNARE complex, assembled from synaptobrevin on the vesicle, syntaxin on the plasma membrane, and SNAP-25, which contributes two of the four helices. Botulinum neurotoxin A paralyses muscle by cleaving SNAP-25, which disables that assembly and stops acetylcholine release at the neuromuscular junction. SNAP-8 and Argireline both copy the N-terminal region of SNAP-25, residues 12 to 19 in the octapeptide's case. The proposal behind them is that a small peptide patterned on this domain competes with native SNAP-25 for complex formation, weakening the fusion machinery that releases acetylcholine and catecholamines.
The Mechanistic Literature
The reference mechanistic study is Blanes-Mira and colleagues (J Neurochem, 2004), who mapped the SNAP-25 N-terminus and identified the segment from Ala22 to Ile44 as essential for SNARE complex formation. They reported that peptides patterned after this domain inhibit SNARE complex assembly, that the inhibition correlates with the peptides' alpha-helical propensity, and that the peptides disrupt the binary SNAP-25/syntaxin complex when added before assembly begins. Functionally, the peptides inhibited calcium-dependent exocytosis in detergent-permeabilised chromaffin cells, the standard model system for catecholamine release, and protected hippocampal neurones against excitotoxicity with a potency rivalling botulinum neurotoxin. The chromaffin cell system itself was established for SNAP-25 peptides by Gutierrez and colleagues (J Biol Chem, 1997), who showed that a C-terminal SNAP-25 peptide blocks secretory vesicle docking. The N-terminal peptide series of the 2004 paper is the mechanistic basis on which the cosmetic octapeptide was developed.
From Argireline to SNAP-8
SNAP-8 exists because of the hexapeptide that preceded it. Blanes-Mira and colleagues (Int J Cosmet Sci, 2002) described Ac-EEMQRR-NH₂, coined Argireline, as a rational design product intended to mimic the anti-wrinkle action of botulinum toxin without its toxicity. In that paper the hexapeptide inhibited neurotransmitter release in vitro, and a 10% oil-in-water emulsion reduced wrinkle depth by up to 30% after 30 days in a small open-label study in healthy women volunteers. The octapeptide was then built by extending the C-terminus with Ala-Asp, matching SNAP-25 residues 18 and 19, on the logic that a longer N-terminal mimic would engage the SNARE interface more effectively. Published head-to-head data comparing the two peptides are sparse, so the relative potency claims that circulate are best treated as manufacturer data rather than established finding.
The Cosmetic Science Context
SNAP-8 is studied primarily in cosmetic science, where it belongs to the class of neurotransmitter-inhibiting peptides catalogued by Pintea and colleagues (Biomolecules, 2025). The conceptual case is straightforward: if a peptide weakens SNARE-dependent exocytosis at the neuromuscular junction, then reduced muscle contraction might reduce the formation of expression lines. That is a model, not an established outcome, and the published evidence for the octapeptide specifically is thin. Its most-quoted efficacy figures come from the manufacturer's technical dossier rather than independent journals, and the peer-reviewed wrinkle-depth data belong to the hexapeptide, not to SNAP-8. Analytical methods for quantifying the peptide in formulations exist (Ji et al., J Anal Sci Technol, 2020), but the efficacy literature an independent laboratory can rely on is small.
Reading the Evidence Honestly
Three structural caveats should be weighed before building a study around SNAP-8. First, the mechanistic literature is small and concentrated in one research group, with the defining papers coming from the same laboratory that designed the peptide; independent replication of the SNARE-interference data is limited. Second, the cosmetic evidence base is mostly manufacturer material, and the one widely quoted clinical figure, a 30% reduction in wrinkle depth, belongs to the hexapeptide's small open-label volunteer study from 2002, which cannot be treated as a randomised controlled trial. Third, SNAP-8 holds no marketing authorisation anywhere and no therapeutic use is established. None of this makes the compound uninteresting; it makes it a tool compound whose evidence base must be read at its actual size. This guide therefore carries no dosing information, no human-use claims and no outcome promises.
Laboratory Handling
Store the lyophilised vial at -20°C, protected from light and moisture. Reconstitute by slowly injecting Bacteriostatic Water down the inner wall of the vial and swirling gently until the solution is clear and colourless; never shake or vortex. The methionine at position three is oxidation-prone, so keep headspace minimal, re-seal promptly and aliquot into single-use volumes rather than repeatedly puncturing one stock. Hold reconstituted solution at 2-8°C and use within 4 weeks. See the peptide storage guide and the reconstitution guide for fuller methodology. For in-vitro laboratory research use only.
Sourcing in the UK
UK Peptide Lab supplies research-grade SNAP-8 10mg at £19.99 as lyophilised powder, supplier-tested, batch UKPL-9511 at 98.92% purity by RP-HPLC, with the certificate of analysis published on the product page and independent third-party verification pending. Same-day UK dispatch on orders before 2pm GMT, free Royal Mail Tracked shipping over £45. SNAP-8 is supplied strictly for in-vitro laboratory research use, is not a licensed medicine anywhere, and purchasers must be 18 or over.
Related Products
Disclaimer: This article is for research and educational purposes only. All information provided is not intended as medical advice. UK Peptide Lab products are not for human consumption and are sold strictly for laboratory research use only.
Frequently Asked Questions
What is SNAP-8?
SNAP-8 (acetyl octapeptide-3) is a synthetic eight-residue peptide, sequence Ac-Glu-Glu-Met-Gln-Arg-Arg-Ala-Asp-NH₂, molecular weight approximately 1075 g/mol, CAS 868844-74-0. It was designed as an extended form of acetyl hexapeptide-3 (Argireline), adding alanine and aspartate at the C-terminus. Both peptides mimic the N-terminal region of SNAP-25, the SNARE complex protein cleaved by botulinum neurotoxin A. Supplied as lyophilised powder for in-vitro laboratory research only.
Does SNAP-8 work like botulinum toxin?
Not in any literal sense. Botulinum neurotoxin A is an enzyme that cleaves SNAP-25; SNAP-8 is a short peptide proposed to compete with SNAP-25 for SNARE complex formation, which in cell models translates into reduced calcium-dependent catecholamine exocytosis (Blanes-Mira et al., J Neurochem, 2004). The published mechanistic work is in vitro; SNAP-8 is a research peptide, not a medicine, and no therapeutic equivalence to botulinum toxin is claimed.
What is the difference between SNAP-8 and Argireline?
Argireline is the six-residue peptide Ac-Glu-Glu-Met-Gln-Arg-Arg-NH₂ (approximately 889 g/mol); SNAP-8 is the same sequence extended with Ala-Asp at the C-terminus (approximately 1075 g/mol, CAS 868844-74-0). The hexapeptide carries the published cosmetic study reporting up to 30% wrinkle-depth reduction in a small open-label volunteer study (Blanes-Mira et al., Int J Cosmet Sci, 2002); published head-to-head data for the octapeptide are sparse.
How is SNAP-8 reconstituted and stored?
Inject bacteriostatic water slowly down the inner glass wall, then swirl gently until the solution is clear and colourless; never shake or vortex. Store lyophilised vials at -20°C, hold reconstituted solution at 2-8°C and use within 4 weeks. The methionine at position three is oxidation-prone, so minimise headspace and aliquot into single-use volumes. Research use only.
References
- [1] Small peptides patterned after the N-terminus domain of SNAP25 inhibit SNARE complex assembly and regulated exocytosis. J Neurochem (2004). View →
- [2] A synthetic hexapeptide (Argireline) with antiwrinkle activity. Int J Cosmet Sci (2002). View →
- [3] A peptide that mimics the C-terminal sequence of SNAP-25 inhibits secretory vesicle docking in chromaffin cells. J Biol Chem (1997). View →
- [4] Peptides: Emerging Candidates for the Prevention and Treatment of Skin Senescence: A Review. Biomolecules (2025). View →
- [5] Method development for acetyl octapeptide-3 analysis by liquid chromatography-tandem mass spectrometry. J Anal Sci Technol (2020). View →