SNAP-8

SNAP-8 is a synthetic octapeptide with the sequence Ac-Glu-Glu-Met-Gln-Arg-Arg-Ala-Asp-NH2, acetylated at the N-terminus and amidated at the C-terminus. Its molecular formula is C41H70N16O16S with a molecular weight of approximately 1075.2 g/mol; PubChem catalogues the structure as CID 76283482 under CAS number 868844-74-0. In cosmetic-ingredient nomenclature it is acetyl octapeptide-3 or acetyl glutamyl heptapeptide-1. The sequence is patterned on the N-terminal region of SNAP-25, a synaptosomal-associated protein of the SNARE family, and is two residues longer than acetyl hexapeptide-8 (Argireline), the earlier ingredient of this class. Material is supplied as a lyophilized (freeze-dried) solid.

SNAP-8 is used as a cosmetic-ingredient and formulation-science research material rather than in therapeutic development. Published work around this class is in vitro or formulation-focused: SNARE assembly assays, secretion assays in cultured cells, and behaviour in emulsions and other vehicles. Supplied here as a reference compound, it is not a finished cosmetic, and this entry describes no appearance-related outcome. Identity figures above should be reconciled against the Certificate of Analysis for the lot in hand. SNAP-8 is sold for research use only and is not for human or veterinary use.

The SNAP-25 fragment approach predates SNAP-8. In 1997 Gutierrez and colleagues reported that a synthetic peptide reproducing the C-terminal sequence of SNAP-25 interfered with secretory vesicle docking in cultured chromaffin cells (PubMed 9006897), showing that short fragments could compete during SNARE assembly.

Blanes-Mira and colleagues then reported that small peptides patterned after the N-terminus domain of SNAP-25 inhibited SNARE complex assembly and exocytosis in cell-free and cellular systems (PubMed 14675156). SNAP-8 is an elongated eight-residue analogue of the hexapeptide from that work. Avcil and colleagues later included acetyl octapeptide-3 as one of five actives in a hyaluronic acid patch formulation (PubMed 31134751).

The evidence base specific to SNAP-8 is thin. Most mechanistic work used the shorter hexapeptide or SNAP-25 fragments generally, and studies naming acetyl octapeptide-3 test it inside multi-ingredient formulations, so component-level attribution is impossible.

The mechanism described is competitive interference with SNARE complex assembly. SNAP-25 forms a ternary complex with syntaxin-1 and VAMP that mediates vesicle fusion, and short peptides reproducing its terminal regions reportedly engage the partner proteins and slow that assembly (PubMed 14675156, PubMed 9006897).

SNAP-25 is also the substrate of clostridial neurotoxins used as laboratory tools in SNARE research; those cleave the protein enzymatically, whereas the peptide fragments here compete non-covalently. SNAP-8 is likewise distinct from GHK-Cu, studied in extracellular matrix pathways rather than exocytosis.

Cell-free assembly and chromaffin-cell secretion assays report molecular events in defined systems, not tissue-level outcomes, and whether a charged octapeptide reaches an intracellular target is what the delivery literature examines (PubMed 25497319). Conditions are defined in each cited study’s methodology.

Sealed lyophilized SNAP-8 is held frozen at -20°C, shielded from light, in its original container. Lyophilized peptides are hygroscopic, so a container reaches ambient temperature before opening. Repeated freeze-thaw cycles are avoided.

Methionine at position 3 is the most oxidation-prone residue, and glutamine at position 4 can deamidate. Stability for a lot is documented on its Certificate of Analysis, not stated as a duration.

Reconstitution means returning a lyophilized compound to solution. This entry gives no preparation procedure: solvent, concentration and handling steps belong to a protocol, not a compound entry. SNAP-8 carries three acidic side chains and two guanidinium groups and is handled as aqueous-soluble material, with apparent solubility strongly pH dependent.

Lyophilized SNAP-8 takes up atmospheric moisture, degrading gravimetric accuracy. Water content, salt form and solubility figures appear on the lot Certificate of Analysis; conditions come from each study’s methodology.

Identity and purity of research-grade SNAP-8 are established analytically, typically by reverse-phase HPLC with mass spectrometric confirmation. Verified purity is documented per lot on the Certificate of Analysis. The analytical questions that matter most are acetylation and amidation completeness, methionine sulfoxide content and deletion impurities at the arginine pair.

Nomenclature is a practical quality issue: several ingredient names circulate for this one sequence, and at least one public database record indexed to SNAP-8 carries a structure differing from the CAS-registered one. Sequence and mass on the Certificate of Analysis are the reliable check.

SNAP-8 is catalogued alongside these compounds in this encyclopedia.

• GHK-Cu.
  Copper-binding tripeptide studied in matrix-remodelling models, the other cosmetic-adjacent research peptide here.
• Acetyl hexapeptide-8 (Argireline).
  Shorter parent research ingredient of this class and the subject of most published work; not catalogued separately.
• KPV.
  Melanocortin-derived tripeptide studied in cultured-cell models.
• GLOW Blend (entry forthcoming).
  Vendor-defined blend built around GHK-Cu.

Gutierrez LM, Viniegra S, Rueda J, et al. (1997). A peptide that mimics the C-terminal sequence of SNAP-25 inhibits secretory vesicle docking in chromaffin cells. J Biol Chem.
PubMed 9006897

Blanes-Mira C, Merino JM, Valera E, et al. (2004). Small peptides patterned after the N-terminus domain of SNAP25 inhibit SNARE complex assembly and regulated exocytosis. J Neurochem.
PubMed 14675156

Hoppel M, Reznicek G, Kahlig H, et al. (2015). Topical delivery of acetyl hexapeptide-8 from different emulsions: influence of emulsion composition and internal structure. Eur J Pharm Sci.
PubMed 25497319

Avcil M, Akman G, Klokkers J, et al. (2020). Efficacy of bioactive peptides loaded on hyaluronic acid microneedle patches: a monocentric clinical study. J Cosmet Dermatol.
PubMed 31134751

SNAP-8 is stocked here in one format: sealed single-compound lyophilized vials from three supplier brands, one of them the house brand Novelle Bio. Vials are the only listed format for this compound, and every listed fill is 10mg. Per-vial strengths are product specifications only. Each lot is batch tested with a published Certificate of Analysis documenting verified purity for that lot.

• Browse all SNAP-8 research products
• Verified Peptides SNAP-8, 10mg lyophilized vial
• Novelle Bio SNAP-8, 10mg lyophilized vial
• Real Peptides SNAP-8, 10mg lyophilized vial
• Collections: Research Vials. Documentation: COA and Lab Testing.

These products are sold for Research Use Only and are not intended for human consumption.