SNAP-8 (10mg)

SNAP-8 (Acetyl Octapeptide-3, also designated Acetyl Glutamyl Heptapeptide-3) is an 8-amino acid synthetic biomimetic peptide with sequence Ac-Glu-Glu-Met-Gln-Arg-Arg-Ala-Asp-NH2. Developed by Lipotec S.A. (Barcelona, Spain; acquired by Lubrizol/Berkshire Hathaway in 2012), SNAP-8 was designed as an advanced topical alternative to botulinum neurotoxin for reduction of dynamic facial wrinkles. The peptide represents a structural elongation of its predecessor Argireline (Acetyl Hexapeptide-8, Ac-EEMQRR-NH2), with two additional amino acid residues (Ala-Asp) appended to the C-terminus, conferring approximately 30% greater anti-wrinkle activity in comparative studies.

SNAP-8 derives its name from its biomimetic relationship with SNAP-25 (Synaptosomal Associated Protein of 25 kDa), a critical component of the SNARE (Soluble N-ethylmaleimide-sensitive factor Attachment protein REceptor) complex responsible for calcium-dependent vesicle fusion and neurotransmitter release at the neuromuscular junction. The N-terminal acetyl cap and C-terminal amide group enhance metabolic stability and reduce susceptibility to aminopeptidase and carboxypeptidase degradation. The sequence contains two glutamic acid residues, one aspartic acid, and two arginine residues, resulting in amphiphilic character that influences aqueous solubility and membrane interaction.

Mechanism of Action: The SNARE complex is a ternary protein assembly essential for calcium-dependent neurotransmitter vesicle fusion, consisting of VAMP/synaptobrevin (vesicle membrane), syntaxin-1 (plasma membrane), and SNAP-25 (plasma membrane-associated). These proteins form a coiled-coil four-helix bundle that draws vesicle and plasma membranes into proximity to drive fusion and neurotransmitter exocytosis. SNAP-8 acts as a biomimetic fragment of the N-terminal SNARE motif of SNAP-25, competitively inhibiting endogenous SNAP-25 incorporation into the ternary SNARE complex.

At 1.5 mM concentration, SNAP-8 achieves approximately 43% inhibition of glutamate release in vitro (Errante et al. 2020). This partial inhibition contrasts fundamentally with botulinum toxin type A, which enzymatically cleaves SNAP-25 via zinc-dependent metalloprotease activity, producing complete and irreversible blockade of neurotransmitter release. SNAP-8's dose-dependent, reversible modulation results in muscle relaxation rather than paralysis, providing a fundamentally different pharmacological profile with superior safety characteristics compared to injectable neurotoxins.

Synergistic Activity: SNAP-8 exhibits synergistic activity when combined with Leuphasyl (Pentapeptide-18). At equimolar concentrations (0.75 mM each), SNAP-8 produces 38% inhibition and Leuphasyl produces 7% inhibition independently; combined administration yields 47% inhibition, exceeding additive prediction. This synergy arises because SNAP-8 targets SNARE complex assembly (presynaptic vesicle fusion machinery) while Leuphasyl operates through opioid receptor-mediated presynaptic inhibition, providing complementary suppression through distinct molecular pathways.

This research-grade peptide is provided at >98% purity for investigations of SNARE complex biology, neurotransmitter release mechanisms, cosmeceutical development, transdermal drug delivery, and neuromuscular junction pharmacology.

This product is intended strictly for research purposes and is not for human or veterinary use.