SNAP-8 (Acetyl Octapeptide-3) – Research Compound | 10mg & 100mg Bulk Kit

Description

Disclaimer: This compound is provided strictly for laboratory and scientific research purposes only. It is not approved by the U.S. Food and Drug Administration (FDA) for human or veterinary use, including ingestion, injection, or any form of administration.

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.

Chemical Properties of the Compound

Shared Properties – Both Variants

SKU-Specific Format

Overview

SNAP-8 (Acetyl Octapeptide-3, Acetyl Glutamyl Heptapeptide-1, CAS 868844-74-0) is a synthetic eight-residue peptide developed by Lipotec (now Lubrizol Life Science) as a structural extension of the Argireline (Acetyl Hexapeptide-3) SNARE-inhibition platform. Its sequence – Ac-Glu-Glu-Met-Gln-Arg-Arg-Ala-Asp-NH₂ – is designed to mimic residues 12–19 of the N-terminal SNARE motif of SNAP-25 (Synaptosomal-Associated Protein 25 kDa), one of the three obligate proteins in the SNARE (Soluble NSF Attachment protein REceptor) complex that drives Ca²⁺-regulated vesicular fusion and neurotransmitter exocytosis at neuromuscular junctions. By presenting this mimetic sequence, SNAP-8 functions as a reversible, non-proteolytic competitive inhibitor of SNARE complex assembly – mechanistically distinct at every level from botulinum neurotoxin. It is an INCI-listed cosmetic ingredient and is not FDA-approved for any drug indication.

BC9 supplies SNAP-8 in two research formats: a 10mg single vial for standard laboratory assay work and a 100mg bulk kit (10 vials, 1000mg total) for cosmetic formulation concentration studies, large-scale SNARE pharmacology dose-response research, and multi-vehicle transdermal delivery investigations. Both formats contain identical compounds at ≥98% purity. This compound is not FDA-approved for human or veterinary use, is not a dietary supplement or consumer product, and is supplied strictly for laboratory and research purposes. Availability is restricted to qualified researchers and licensed laboratory institutions. IRB guidance is required for clinical research initiatives. IACUC compliance is required for preclinical animal research.

Working Mechanism of SNAP-8

SNARE Complex Architecture and the Role of SNAP-25: The SNARE complex is a four-helix coiled-coil bundle assembled from three proteins: syntaxin-1 (a Qa-SNARE on the presynaptic plasma membrane), SNAP-25 (a Qb+Qc-SNARE contributing two SNARE motifs via its N-terminal and C-terminal alpha-helices), and VAMP/synaptobrevin (an R-SNARE on the secretory vesicle membrane). Complex formation proceeds directionally from the N-terminal end of the SNARE motifs toward the C-terminal membrane-proximal region – a process described as ‘zippering’. This zippering action draws the vesicle membrane into nanometre-range proximity of the plasma membrane, overcoming the energy barrier for lipid bilayer fusion and driving Ca²⁺-triggered acetylcholine exocytosis at the neuromuscular junction.

SNAP-8 as a Competitive SNAP-25 N-Terminal Mimic: SNAP-8’s sequence (Ac-EEMQRR-AA-D-NH₂) corresponds to SNAP-25 residues 12–19 of the first SNARE motif – the N-terminal alpha-helix that contributes one of the four strands in the coiled-coil bundle. By presenting this coiled-coil interaction interface, SNAP-8 competes with native SNAP-25 for docking positions within the assembling SNARE complex – specifically for complementary interactions with syntaxin-1 and VAMP/synaptobrevin. This competitive occupancy reduces the probability of productive SNARE complex nucleation, attenuating assembly efficiency without cleaving any component protein. The result is dose-dependent inhibition of Ca²⁺-dependent vesicle-membrane fusion kinetics and reduced acetylcholine release in in vitro neuromuscular junction and chromaffin cell exocytosis model systems.

Extension of the Argireline Platform – Two Additional C-Terminal Residues: Argireline (Acetyl Hexapeptide-3, Ac-EEMQRR-NH₂) mimics SNAP-25 residues 12–17. SNAP-8 extends this by two residues (Ala-Asp at positions 18–19), increasing the SNARE interaction interface presented to the assembling complex. In vitro chromaffin cell exocytosis data (Blanes-Mira et al. 2002, PMID 18498523, for the Argireline class) document dose-dependent catecholamine release inhibition via this SNARE competitive mechanism. SNAP-8’s extended octapeptide sequence achieves greater SNARE complex competitive binding than the hexapeptide at equivalent concentrations in published comparative in vitro data, attributed to the additional coiled-coil surface contacts provided by the Ala-Asp extension.

Critical Mechanistic Distinction from Botulinum Toxin: Botulinum neurotoxin serotypes A and E cleave SNAP-25 irreversibly at specific Gln-Arg and Arg-Ile peptide bonds via zinc-dependent metalloprotease catalytic activity, permanently eliminating that SNAP-25 molecule’s ability to participate in SNARE complex formation. SNAP-8’s competitive inhibition is pharmacologically reversible, concentration-dependent, and requires no enzymatic activity. This mechanistic distinction makes SNAP-8 an appropriate tool compound for investigating competitive SNARE modulation in the absence of the protease-mediated irreversibility and off-target effects that complicate botulinum toxin-based experimental designs.

Bulk Kit (100mg) Additional Research Utility: At 100mg per vial (1000mg total), the bulk kit format enables: (1) cosmetic formulation concentration optimization at industry-research-standard 1–10% (w/v) concentrations in aqueous serum and cream vehicles, where per-experiment consumption is high; (2) full SNARE inhibition dose-response curve construction from picomolar to millimolar concentrations across multiple chromaffin cell or PC12 exocytosis experimental replicates; (3) parallel multi-vehicle transdermal delivery comparison across liposomal, nanoparticle, and microemulsion systems from a single matched batch.

Research Findings / Research Applications

Preclinical investigations have examined SNAP-8 in relation to:

•       SNARE complex competitive inhibition pharmacology (both variants): SNAP-8 is investigated as a tool compound for probing the structural requirements for SNAP-25 N-terminal SNARE motif contributions to coiled-coil nucleation and assembly kinetics in cell-free reconstitution assays and transfected neuronal cell models. The 10mg vial is calibrated for standard SNARE pharmacology assays; the 100mg bulk kit supports comprehensive inhibition curve construction from sub-inhibitory to saturating concentrations.
•       Neuromuscular junction acetylcholine release modulation (both variants): In vitro chromaffin cell, PC12 cell, and synaptosome exocytosis assay systems use SNAP-8 as a competitive inhibitor to investigate Ca²⁺-dependent vesicle fusion kinetics and catecholamine release inhibition at defined peptide concentrations. The Argireline class mechanism (Blanes-Mira et al. 2002, PMID 18498523) provides the pharmacological framework for SNAP-8 SNARE inhibition research.
•       Cosmetic peptide transdermal delivery research (bulk kit primarily): In ex vivo skin barrier models and Franz diffusion cell systems, SNAP-8 is investigated for permeation across stratum corneum and dermis. Comparative penetration enhancement research using liposomal, nanoparticle, and microemulsion delivery vehicles consumes higher peptide quantities per experiment – making the 100mg bulk kit the appropriate format for this application area.
•       Structure-activity relationship (SAR) comparative research (bulk kit primarily): SNAP-8 vs Argireline parallel SAR investigation – examining how the two additional C-terminal Ala-Asp residues alter SNARE complex competitive binding affinity and inhibition potency relative to the hexapeptide – requires multi-concentration, multi-replicate matched-batch material best served by the bulk kit format.

Note: These findings are based on early-stage and preclinical research. Results are not consistent across all models, and data remain limited without validation in human clinical settings.

Risks & Handling Information

•       The use of appropriate personal protective equipment (PPE) is essential in conducting experiments involving SNAP-8. Nitrile gloves, a laboratory coat, and eye protection are required at a minimum. For the 100mg bulk kit, a fume hood or appropriate powder-handling containment is recommended during vial opening and dry powder transfer to avoid fine lyophilized powder aerosol inhalation.
•       Handling should occur within controlled laboratory environments designed for research activities. For cosmetic formulation research at 1–10% concentrations, use appropriate formulation-grade vehicles and aseptic technique throughout.
•       Do not inhale, ingest, or make direct skin contact with the compound in concentrated lyophilized or reconstituted form. SNAP-8 is a SNARE complex modulator; its activity profile in non-target biological systems has not been fully characterized.
•       The toxicological profile of SNAP-8 at research concentrations exceeding cosmetic-grade topical-use levels is not fully established. Exposure risks remain uncertain due to limited long-term safety data for either vial format at injectable or concentrated solution concentrations. No human safety data has been established for research-grade SNAP-8 at the concentrations supplied.
•       Improper storage conditions, including exposure to heat, light, or moisture, may result in compound degradation and compromised sample integrity. Store lyophilized vials at −20°C in sealed, light-protected containers. Reconstituted solution: use within 4 weeks at 2–8°C. Avoid repeated freeze-thaw cycles.

FAQs

What is the difference between the 10mg vial and the 100mg bulk kit?

Both contain identical SNAP-8 (Acetyl Octapeptide-3) at ≥98% purity with the same mechanism and INCI listing. The 10mg vial is calibrated for standard SNARE pharmacology assays (cAMP accumulation, chromaffin cell exocytosis, PC12 catecholamine release) and small-scale skin model research at the laboratory assay scale. The 100mg bulk kit (1000mg total across 10 vials) is designed for cosmetic formulation concentration optimization at 1–10% (w/v) in multiple vehicle systems, comprehensive inhibition dose-response curve construction, multi-vehicle transdermal delivery comparison, and large-scale SAR studies requiring matched-batch material across multiple experimental conditions.

How does SNAP-8 differ from Argireline (Acetyl Hexapeptide-3) in SNARE research?

Argireline mimics SNAP-25 residues 12–17 (6 residues: Ac-EEMQRR-NH₂). SNAP-8 extends the mimic to residues 12–19 (8 residues: Ac-EEMQRR-AD-NH₂), adding Ala-Asp at the C-terminus. These two additional residues extend the coiled-coil surface presented to the assembling SNARE complex, producing greater competitive binding in published in vitro chromaffin cell data (Blanes-Mira et al. 2002 for Argireline class; SNAP-8 comparative data). SNAP-8 is therefore the appropriate compound when higher SNARE inhibition potency relative to the hexapeptide standard is the research objective.

Is SNAP-8 mechanistically related to botulinum toxin?

No. Botulinum toxin serotypes A and E are zinc-dependent metalloprotease enzymes that irreversibly cleave SNAP-25 at defined peptide bonds, permanently destroying that SNAP-25 molecule’s capacity for SNARE complex participation. SNAP-8 is a reversible competitive inhibitor – it competes with native SNAP-25 for SNARE complex assembly sites without enzymatic activity or proteolytic cleavage. The mechanisms are pharmacologically distinct at every level.

What storage and stability conditions apply to both variants?

Store both lyophilized variants (10mg vial and 100mg bulk kit) 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 conditions.

Is SNAP-8 FDA-approved?

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

What concentrations are investigated in cosmetic formulation research?

Published cosmetic formulation literature has investigated the Argireline class (which SNAP-8 extends) at 1–10% (w/v) concentrations in aqueous serum and cream vehicles. At these concentrations, per-experiment reagent consumption is substantially higher than for cell-based pharmacology assays – which is the primary rationale for the 100mg bulk kit format for this application area. The 10mg vial is not sufficient for multi-vehicle, multi-concentration formulation optimization from a single matched batch.

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/
•       Apland JP, Adler M, Oyler GA. Inhibition of neurotransmitter release by peptides that mimic the N-terminal domain of SNAP-25. J Protein Chem. 2003;22(2):147–153. PMID: 12760419. https://pubmed.ncbi.nlm.nih.gov/12760419/

Nguyen TQ, Zahr AS, Kononov T, Ablon G. A randomized, double-blind, placebo-controlled clinical study investigating the efficacy and tolerability of a peptide serum targeting expression lines. J Clin Aesthet Dermatol. 2021;14(5):14–21. PMID: 34188744. https://pubmed.ncbi.nlm.nih.gov/34188744/ 

This content is presented exclusively for educational purposes and should not be construed as medical advice. THE MATERIALS REFERENCED HEREIN ARE EXCLUSIVELY INTENDED FOR LABORATORY AND RESEARCH USE.

Any clinical research initiatives must be conducted under the guidance of the relevant Institutional Review Board (IRB). Similarly, preclinical research involving animals must comply with the directives of the Institutional Animal Care and Use Committee (IACUC), adhering to the standards delineated by the Animal Welfare Act (AWA).

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