Scientific Reference
SNAP-8 (Acetyl Octapeptide-3)
Evidence profile: No indexed evidence identified
SNAP-8, or acetyl octapeptide-3, is a synthetic eight-residue peptide modelled on the N-terminal region of the neuronal protein SNAP-25. Its sequence, Glu-Glu-Met-Gln-Arg-Arg-Ala-Asp, extends the related acetyl hexapeptide-3 by two residues, and both ends are capped: acetylated at the N-terminus and amidated at the C-terminus. It was developed as a cosmetic ingredient, and most available data come from ingredient-level testing and small studies of topical formulations rather than independent research. Biochemical work has looked at its interaction with the SNARE complex in vitro. Whether a peptide of this size crosses intact skin to reach nerve terminals in meaningful amounts has not been well established.
Mechanism of Action
Release of neurotransmitter from a nerve terminal depends on the SNARE complex, a bundle of helices contributed by SNAP-25, syntaxin and synaptobrevin (VAMP) that draws vesicle and plasma membranes together. Acetyl octapeptide-3 copies a short stretch of the SNAP-25 N-terminus and has been proposed to compete with the native protein for a place in that bundle. Reports, mostly from ingredient developers, describe less efficient assembly of stable complexes and reduced neurotransmitter release from cultured cells. These data come largely from simplified systems, and evidence that the same interaction occurs in intact tissue is limited.
Molecular Information
- Type: Acetylated octapeptide with C-terminal amidation
- Length: 8 amino acids
- Molecular weight: 1075.2 g/mol
- Molecular formula: C41H70N16O16S
- CAS: 868844-74-0