SNAP-8

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.

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.

UK Peptide Lab 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.