SNAP-8's proposed mechanism involves competition with SNAP-25 for incorporation into the SNARE complex — the molecular machinery that fuses neurotransmitter vesicles with the presynaptic membrane. In cell-free and cell culture assays, SNAP-8 has been shown to reduce the efficiency of SNARE complex formation, which theoretically decreases acetylcholine release at the neuromuscular junction.1
AESTHETICS
SNAP-8
$34.99
SNAP-8 is an acetylated octapeptide analog of the N-terminal domain of SNAP-25. It is used in vitro to investigate SNARE complex interactions, synaptic vesicle fusion, and peptide-mediated modulation of exocytosis in neuromuscular and dermal models, supporting structure–activity and vesicle trafficking research under controlled conditions.
QuantityStandard research vial
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Product Overview
SNAP-8 (acetyl octapeptide-3) is a synthetic peptide designed to mimic the N-terminal end of SNAP-25 — a protein that forms part of the SNARE complex responsible for neurotransmitter release at neuromuscular junctions. By competing with native SNAP-25, the peptide is hypothesized to modulate the SNARE complex assembly, reducing neuromuscular activity in the muscle fibers responsible for expression-line formation.
SNAP-8 is an extension of the SNAP-6 concept (acetyl hexapeptide-3, also known as Argireline), with two additional amino acids that may improve receptor binding and potency. It is studied exclusively in the aesthetics/cosmetics research context — its entire research profile centers on the molecular biology of facial expression wrinkle formation.
Research Applications
Mechanism and Experimental Context
SNAP-8 is studied in cell culture models of expression-line biology, including primary keratinocyte and fibroblast cultures from facial skin. Research measures the effect of SNAP-8 treatment on cellular contractility markers and extracellular matrix organization in these models.2
SNAP-8 is widely studied in the cosmeceutical research field as a peptide-based approach to expression line reduction. It represents the pharmaceutical chemistry approach to understanding how small peptides can modulate specific molecular targets in skin biology.
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Referenced Studies
Source Literature
[1]
Blanes-Mira C, et al. "A synthetic hexapeptide (Argireline) with antiwrinkle activity." International Journal of Cosmetic Science, 2002. PubMed: PMID 18498517
[2]
Wang Y, et al. "Anti-wrinkle efficacy of acetyl octapeptide-3." Journal of Cosmetic Dermatology, 2013.
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Batch Documentation
Current published batch documentation is surfaced on-page whenever the provider exposes a public COA asset.
Frequently Asked Questions
Questions About SNAP-8
SNAP-8 (acetyl octapeptide-3) is a synthetic peptide that mimics SNAP-25, a component of the SNARE complex at neuromuscular junctions. It is studied for its potential to modulate neuromuscular signaling in expression-line research models.
The SNARE complex is molecular machinery that enables neurotransmitter vesicles to fuse with the cell membrane and release their contents. It consists of three proteins: SNAP-25, syntaxin, and VAMP. SNAP-8 is designed to interfere with SNAP-25's role in this complex.
Argireline (acetyl hexapeptide-3) is the 6-amino-acid predecessor. SNAP-8 is the 8-amino-acid version with two additional residues that may improve binding. Both target the same SNARE complex mechanism.
No. SNAP-8 is a research compound sold for laboratory research only.
Its entire research profile is specific to expression-line biology and cosmeceutical science. Unlike other OSYRIS compounds that span multiple research areas, SNAP-8's applications are exclusively in the aesthetics/dermatology context.
Store at 2-8°C, protected from light.
Independently tested via HPLC and LC-MS. COA downloadable on this page.
OSYRIS SNAP-8 is supplied at 500mg. Research protocols vary — consult published literature for relevant concentrations in cell culture and in vitro models.
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