SNAP-8 (Acetyl Octapeptide-3)

Available SKUs - 2 Variants: SNAP-8 10mg per vial (single vial) · SNAP-8 100mg per vial, 10-vial bulk kit (1000mg total). Identical compound, purity, and mechanism. Differentiated by vial mass and kit volume for different research programme scales.

What is SNAP-8 (Acetyl Octapeptide-3)?

SNAP-8 (Acetyl Octapeptide-3, Acetyl Glutamyl Heptapeptide-1, CAS 868844-74-0) is a synthetic eight-residue peptide - Ac-Glu-Glu-Met-Gln-Arg-Arg-Ala-Asp-NH₂ - originally developed by Lipotec (now Lubrizol Life Science) as a structural extension of the well-characterised Argireline (Acetyl Hexapeptide-3) SNARE-inhibition platform. Positioned within the SNARE complex modulator class of cosmetic research peptides, SNAP-8 functions as a reversible, non-proteolytic competitive inhibitor of SNARE complex assembly by mimicking residues 12–19 of the N-terminal SNARE motif of SNAP-25 (Synaptosomal-Associated Protein 25 kDa). The two additional C-terminal residues (Ala-Asp) distinguishing SNAP-8 from the hexapeptide Argireline expand the SNARE coiled-coil interaction interface, producing measurably greater competitive binding in published in vitro data. SNAP-8 is an INCI-listed cosmetic ingredient and is not an FDA-approved drug or therapeutic agent.

RCDbio supplies SNAP-8 in two research formats: a 10mg vial for standard neuromuscular junction and SNARE pharmacology assay work, and a 100mg bulk kit (10 vials, 1000mg total) for cosmetic formulation concentration studies, large-scale exocytosis dose-response investigations, and transdermal delivery research. This compound is not approved by the U.S. FDA for human or veterinary use. It is intended for laboratory and research purposes only, is not a dietary supplement or consumer product, and is available exclusively to qualified researchers and licensed laboratory institutions.

Chemical Properties

Shared Properties - Both Variants

SKU Format Details

How Does SNAP-8 Work?

SNARE Complex Assembly - The Target Molecular Machinery: The SNARE complex constitutes the fundamental molecular engine for Ca²⁺-regulated secretory vesicle fusion at the neuromuscular junction and other synaptic specializations. Its assembly draws together three proteins across two membranes: syntaxin-1 (Qa-SNARE, plasma membrane), SNAP-25 (Qb+Qc-SNARE, plasma membrane, contributing two SNARE motifs), and VAMP/synaptobrevin (R-SNARE, vesicle membrane). Assembly proceeds N-to-C terminally via a 'zippering' mechanism that progressively tightens the four-helix coiled-coil bundle, generating the mechanical energy to merge the apposed lipid bilayers and release vesicle contents into the synaptic cleft. The N-terminal SNARE motif of SNAP-25 - specifically residues 12–19 - is the region targeted by the Argireline/SNAP-8 class of competitive inhibitors.

SNAP-8's Competitive SNAP-25 Mimicry at the SNARE Interface: Investigated in chromaffin cell and transfected cell model systems, SNAP-8 is observed to competitively displace native SNAP-25 from forming SNARE complexes by presenting an identical coiled-coil binding interface. The peptide's Ac-Glu-Glu-Met-Gln-Arg-Arg-Ala-Asp-NH₂ sequence directly mirrors SNAP-25 positions 12–19, occupying the SNARE complex docking site that native SNAP-25 would otherwise fill during productive complex zipping. Occupancy of this site by SNAP-8 reduces SNARE complex assembly efficiency in a concentration-dependent and pharmacologically reversible manner - attenuating Ca²⁺-triggered vesicle-membrane fusion kinetics and catecholamine exocytosis in adrenal chromaffin cell preparations. Inhibition does not involve any enzymatic mechanism, proteolytic cleavage, or covalent modification of SNARE proteins.

Octapeptide vs Hexapeptide - Mechanistic Basis for Greater SNARE Inhibition: The Argireline hexapeptide (Ac-EEMQRR-NH₂) spans SNAP-25 residues 12–17. SNAP-8 extends this by two residues to positions 18–19 (Ala at 18, Asp at 19). In the context of the four-helix coiled-coil bundle, positions 18–19 contribute additional complementary contacts with syntaxin-1 and VAMP/synaptobrevin strands. The extended contact surface increases competitive occupancy probability at equivalent peptide concentrations in in vitro chromaffin cell exocytosis assay systems (Blanes-Mira et al. 2002, PMID 18498523, for Argireline class mechanism). Structurally, both N-terminal acetylation and C-terminal amidation of SNAP-8 are functionally significant: acetylation removes the free α-amino group that would otherwise disrupt helical dipole orientation within the coiled-coil interface, while amidation removes the C-terminal carboxylate charge that could impair hydrophobic core packing.

Reversibility and Mechanistic Distinction from Botulinum Toxin: SNAP-8's inhibition of SNARE assembly has been characterized as fully reversible and concentration-dependent in model systems - consistent with competitive, non-covalent occupancy of the SNARE coiled-coil interface. This pharmacological profile stands in contrast to botulinum neurotoxin serotypes A (BoNT/A) and E (BoNT/E), which function as zinc-dependent endopeptidases that catalytically cleave SNAP-25 at the Gln197-Arg198 (BoNT/A) and Arg180-Ile181 (BoNT/E) peptide bonds. BoNT cleavage permanently eliminates the cleaved SNAP-25 fragment's SNARE-forming capacity regardless of compound concentration or washout. SNAP-8 produces no such irreversible effects, making it an appropriate pharmacological probe for studying competitive SNARE modulation independently of the protease-mediated mechanism operative with BoNT-based experimental tools.

What are the Potential Research Applications of SNAP-8?

SNAP-8 10mg - Standard Assay Research

• SNARE complex assembly kinetics and competitive inhibition pharmacology: SNAP-8 is investigated as a pharmacological probe for SNARE coiled-coil nucleation and assembly dynamics in cell-free reconstitution systems and neuronal cell models. The 10mg format provides sufficient material for dose-response inhibition characterization across 4–6 concentration points in chromaffin cell catecholamine release or PC12 exocytosis assay systems
• Neuromuscular junction Ca²⁺-dependent exocytosis research: In vitro NMJ and chromaffin cell models have been investigated with SNAP-8 to quantify competitive inhibition of vesicle-membrane fusion kinetics. This application is the core pharmacological research use case for the 10mg vial format at standard assay volumes
• SNAP-8 vs Argireline comparative SAR pilot studies: Small-scale comparative investigation of octapeptide vs hexapeptide SNARE inhibition potency at matched concentrations in cell-free and chromaffin cell systems - probing the mechanistic contribution of the Ala-Asp C-terminal extension to coiled-coil competitive binding

SNAP-8 100mg Bulk Kit - Large-Scale and Formulation Research

• Cosmetic formulation concentration optimization: At industry-research-standard concentrations of 1–10% (w/v) in aqueous cream, serum, and emulsion vehicles, per-experiment reagent consumption is substantially higher than for cell-based pharmacology assays. The 100 mg per vial format (1000mg total) enables multi-concentration, multi-vehicle formulation optimization from a single matched batch - investigating aqueous, liposomal, nanoparticle, and microemulsion delivery systems in parallel
• Comprehensive SNARE inhibition dose-response construction: 1000mg total enables construction of full sigmoidal inhibition curves spanning picomolar to millimolar SNAP-8 concentrations in chromaffin cell or synaptosome exocytosis assay systems across multiple independent experimental replicates - providing robust IC50 determination and Hill coefficient characterization for SNARE complex competitive inhibition
• Multi-vehicle transdermal penetration research: Ex vivo skin barrier and Franz diffusion cell studies comparing SNAP-8 penetration across liposomal, nanoparticle, and microemulsion carriers consume per-experiment quantities that make the 100mg bulk kit the appropriate format - enabling same-batch comparison across multiple vehicle conditions simultaneously

What are the Potential Side Effects of SNAP-8?

• No significant acute toxicity has been documented for SNAP-8 at cosmetic-range concentrations in published in vitro chromaffin cell or ex vivo skin model data
• The toxicological profile of SNAP-8 at research concentrations substantially exceeding cosmetic topical-use levels - particularly in reconstituted injectable or concentrated aqueous solution form - is not fully characterized in peer-reviewed literature
• Competitive SNARE inhibition documented in chromaffin cell models is pharmacologically reversible; no permanent or protease-mediated neurotoxic effects analogous to botulinum toxin have been observed in published SNAP-8 literature
• At bulk-kit research concentrations (100mg/vial), lyophilized powder aerosol inhalation during vial handling represents an inhalation risk of indeterminate consequence; appropriate containment is required
• Data remains limited, and findings are not consistent across all model systems. No human safety data has been established for research-grade SNAP-8 at either the 10mg or 100mg vial concentrations

Risk & Handling

Handling Precautions

• Trained laboratory personnel only in a controlled laboratory environment
• PPE: nitrile gloves, laboratory coat, and eye protection required at minimum. For the 100mg bulk kit, use a fume hood or powder-handling containment during lyophilized powder weighing and transfer to prevent fine aerosol inhalation
• Reconstitute under aseptic conditions with sterile water or aqueous buffer. For cosmetic formulation research, use appropriate formulation-grade vehicles

Exposure Risks

• Risk Tier: LOW - no acute toxicity documented at cosmetic or standard assay research concentrations. The 100mg bulk kit requires elevated handling caution relative to the 10mg vial due to higher per-vial powder mass and greater aerosol generation risk during open-vial handling. No human safety data has been established for research-grade SNAP-8 at either vial format concentration. Toxicological profile at concentrations exceeding cosmetic-range topical use is incompletely characterized in the published literature

Storage

• Store both lyophilized variants at −20°C in sealed, light-protected containers
• Reconstituted aqueous solution: stable for approximately 4 weeks at 2–8°C; avoid repeated freeze-thaw cycles
• Stable ≥24 months, lyophilized under recommended storage conditions for both the 10mg vial and 100mg bulk kit

FAQs

What research applications distinguish the 10mg vial from the 100mg bulk kit?

The 10mg vial is calibrated for standard SNARE pharmacology assays (chromaffin cell catecholamine release, PC12 exocytosis, cell-free SNARE reconstitution) and small-scale skin model investigations at typical assay volumes. The 100mg bulk kit (1000mg total) is designed for applications consuming higher quantities per experiment: cosmetic formulation concentration optimization at 1–10% (w/v) in multiple vehicle systems, comprehensive dose-response inhibition curve construction across many concentration points and replicates, and parallel multi-vehicle transdermal delivery comparison from a single matched batch.

How does SNAP-8 mechanistically compare to Argireline within the SNARE inhibitor class?

Within the SNAP-25 N-terminal mimic peptide class, Argireline (Acetyl Hexapeptide-3) represents the six-residue (12–17) progenitor and SNAP-8 the eight-residue (12–19) extension. The Ala-Asp C-terminal addition in SNAP-8 extends the SNARE coiled-coil contact surface, producing measurably greater competitive SNARE complex inhibition in chromaffin cell exocytosis assay systems at equivalent concentrations (Blanes-Mira et al. 2002 for Argireline class; SNAP-8 class comparative data). SNAP-8 is therefore the appropriate compound when SNARE inhibition potency exceeding the hexapeptide standard is the research target.

Is SNAP-8's SNARE inhibition reversible?

Competitive SNARE inhibition by SNAP-8 is documented as pharmacologically reversible and concentration-dependent in published model systems - consistent with non-covalent, non-enzymatic SNARE coiled-coil interface competition. Upon SNAP-8 removal (washout or dilution), normal SNARE complex reassembly and vesicular fusion can resume. This reversibility distinguishes SNAP-8 from botulinum neurotoxin, which produces irreversible SNAP-25 cleavage.

What are the storage and stability requirements for both kit formats?

Store both lyophilized variants (10mg and 100mg bulk kit) at −20°C in sealed, light-protected containers. Reconstituted aqueous solution is stable for approximately 4 weeks at 2–8°C. Avoid repeated freeze-thaw cycles of reconstituted material. Both formats are stable for ≥24 months when lyophilized under recommended storage conditions.

Is SNAP-8 FDA-approved or a pharmaceutical drug?

No. SNAP-8 is an INCI-listed cosmetic ingredient. It is not FDA-approved for any drug or therapeutic indication in either the 10mg or 100mg bulk kit format. Both are research reagents for laboratory use only.

References

• Blanes-Mira C, Clemente J, Jodas G, et al. A synthetic hexapeptide (Argireline) with antiwrinkle activity. International Journal of Cosmetic Science. 2002;24(5):303–310. https://pubmed.ncbi.nlm.nih.gov/18498523/
• Blanes-Mira C et al. Small peptides patterned after the N-terminus domain of SNAP25 inhibit SNARE complex assembly and regulated exocytosis. J Neurochem. 2004;88(1):124–35. PMID 14675156.

Disclaimer: SNAP-8 (Acetyl Octapeptide-3) is exclusively for laboratory research purposes. RCDbio products are not intended to diagnose, prevent, treat, or cure any disease or medical condition.

The Food and Drug Administration has not evaluated the statements on our website. This product is not approved for human or veterinary use. Researchers must comply with all applicable local, state, and federal laws and regulations governing the purchase and use of research compounds. By purchasing, you agree to our Terms and Conditions. RCDbio reserves the right to refuse sales to unauthorized individuals.

ATTENTION: All RCDbio products are strictly for LABORATORY AND RESEARCH PURPOSES ONLY. They are not intended for human consumption, veterinary use, or any other non-research application. For queries, complaints, or support, contact support@rcdbio.co