SNAP-8 10mg

What is SNAP-8 ?

SNAP-8 is an acetyl octapeptide (Glu-Glu-Met-Gln-Arg-Arg-Ala-Asp-NH2) designed to extend the sequence of acetyl hexapeptide-3. Research has examined its reported inhibition of SNARE complex formation and catecholamine release in models of neuromuscular signalling, with applications studied primarily in cosmetic science.

SNAP-8, catalogued as acetyl octapeptide-3, has the sequence Ac-Glu-Glu-Met-Gln-Arg-Arg-Ala-Asp-NH₂. Its formula is C₄₁H₇₀N₁₆O₁₆S, its molecular weight about 1075 g/mol and its CAS number 868844-74-0. It was designed for cosmetic science as an extension of acetyl hexapeptide-3 (Argireline), with alanine and aspartate added at the C-terminus. It is a cosmetic ingredient, not a medicine.

Both peptides copy the N-terminal region of SNAP-25, the 25 kDa protein that gives two helices to the neuronal SNARE complex. That four-helix complex drives calcium-dependent vesicle fusion, and botulinum neurotoxin A cleaves SNAP-25 at the neuromuscular junction. Each SNAP-8 10mg vial holds white lyophilised powder.

SNAP-8 Research Applications

• SNARE assembly : Blanes-Mira and colleagues (J Neurochem, 2004) reported that peptides patterned on the SNAP-25 N-terminus are potent inhibitors of SNARE complex formation.
• Where it acts : in that study SNARE complex formation needed SNAP-25 residues 22 to 44, and inhibition tracked each peptide's tendency to form an alpha-helix. SNAP-8 covers residues 12 to 19 and was not tested there.
• Exocytosis : the same peptides inhibited calcium-dependent exocytosis from detergent-permeabilised excitable cells.
• C-terminal comparison : Gutierrez and colleagues (J Biol Chem, 1997) showed that a 20-residue peptide from the SNAP-25 C-terminus blocked vesicle docking in chromaffin cells, mimicking botulinum toxin A.
• Formulation analysis : published methods quantify the peptide in cosmetic formulations (Ji et al., J Anal Sci Technol, 2020).

Typical in-vitro work covers SNARE assembly assays, competition against native SNAP-25 and syntaxin, and exocytosis models. In cosmetic science it belongs to the neurotransmitter-inhibitor peptides, one of the classes catalogued by Pintea and colleagues (Biomolecules, 2025). Poor membrane permeability is a known limit of that class. The mechanistic literature is small and comes mostly from one group.

SNAP-8 vs Argireline (Acetyl Hexapeptide-3)

The two share six residues. Argireline is Ac-Glu-Glu-Met-Gln-Arg-Arg-NH₂, about 889 g/mol. SNAP-8 adds Ala-Asp at the C-terminus, reaching about 1075 g/mol and matching SNAP-25 residues 12 to 19. Both are proposed to compete with native SNAP-25 for SNARE complex assembly. The published record separates them. The hexapeptide has its own paper, with in-vitro release data and a volunteer study (Blanes-Mira et al., Int J Cosmet Sci, 2002). It inhibited neurotransmitter release with a potency similar to botulinum toxin A, but with much lower efficacy. The octapeptide has no comparable paper of its own; its case rests on the same group's work on N-terminal SNAP-25 peptides (J Neurochem, 2004) and on manufacturer dossiers. Head-to-head data are sparse, so the Ala-Asp extension is the variable under test.

Research Overview

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, molecular formula C₄₁H₇₀N₁₆O₁₆S and molecular weight approximately 1075 g/mol (CAS 868844-74-0). It was designed as an extended form of acetyl hexapeptide-3 (Argireline), the six-residue peptide Ac-Glu-Glu-Met-Gln-Arg-Arg-NH₂, by adding an alanine and an aspartate at the C-terminus, and it was developed and marketed for cosmetic science by Lipotec. Both sequences are patterned after the N-terminal region of SNAP-25, the synaptosome-associated 25 kDa protein of the neuronal SNARE complex. SNAP-25 contributes two helices to this four-helix assembly, which drives calcium-dependent vesicle fusion at the synapse, and it is the substrate cleaved by botulinum neurotoxin A at the neuromuscular junction. Peptides that mimic its N-terminal domain are proposed to compete with native SNAP-25 for complex formation. The reference mechanistic work is Blanes-Mira and colleagues (J Neurochem, 2004), who reported that such peptides inhibit SNARE complex assembly and calcium-dependent catecholamine exocytosis in chromaffin cell models. Research interest in SNAP-8 is therefore centred on models of neuromuscular signalling, with applications studied primarily in cosmetic science as a botulinum-toxin-mimetic model peptide, a class catalogued by Pintea and colleagues (Biomolecules, 2025).

The chromaffin cell model that underpins this field predates the peptide itself: Gutierrez and colleagues (J Biol Chem, 1997) used C-terminal SNAP-25 peptides to block secretory vesicle docking in chromaffin cells, establishing the experimental system in which the later N-terminal peptide series was characterised.

The honest boundary of the evidence is worth stating plainly. The peer-reviewed mechanistic literature is small and originates largely from a single research group. The octapeptide has no published, independent, randomised cosmetic trial of its own; most efficacy figures circulating for it trace to manufacturer technical dossiers rather than journals. And the widely quoted 30% wrinkle-depth figure belongs to the hexapeptide's small open-label volunteer study (Blanes-Mira et al., Int J Cosmet Sci, 2002), not to the octapeptide. SNAP-8 holds no marketing authorisation in any jurisdiction and is supplied as lyophilised powder for in-vitro laboratory research only.

Peptaro supplies SNAP-8 10mg at £19.99, batch UKPL-9511, supplier-tested at 98.92% purity by RP-HPLC, with the certificate of analysis published on this page and independent third-party verification pending.

Storage and Reconstitution

Move vials to the freezer on arrival; the powder tolerates short transit at room temperature. Oxidation of methionine 3 is the main risk in solution. Keep vials tightly sealed with little headspace, protect them from light, and freeze single-use aliquots for longer storage. Discard any solution that turns cloudy.

Vials are sold on their own, without bacteriostatic water for mixing or other supplies.

How to reconstitute and handle

• The sequence carries a methionine at position three, so oxidation is the degradation route to design against. Minimise headspace and stopper-open time, keep solutions cold, and prepare single-use aliquots rather than repeatedly accessing one vial.

For the full method, see the peptide reconstitution guide and the reconstitution calculator.

Research References

• Small peptides patterned after the N-terminus domain of SNAP25 inhibit SNARE complex assembly and regulated exocytosis (Blanes-Mira et al., J Neurochem, 2004)
• A synthetic hexapeptide (Argireline) with antiwrinkle activity (Blanes-Mira et al., Int J Cosmet Sci, 2002)

Published research on SNAP-8 is indexed on PubMed. See our full UK buyer's guide for SNAP-8.