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SNAP-8 (10mg)
SNAP-8 (Acetyl Octapeptide-3) is an 8-amino acid biomimetic peptide (Ac-EEMQRRAD-NH2) that competitively inhibits SNAP-25 incorporation into the SNARE complex, achieving ~43% inhibition of glutamate release. Developed as a topical alternative to botulinum toxin, it provides muscle relaxation (not paralysis) with reversible, dose-dependent modulation of neurotransmitter release.
- Metabolic Synergy Research
- In-Vitro Receptor Profiling
- HPLC Verified (≥98% Purity)
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Research Overview
SNAP-8 (Acetyl Octapeptide-3, Acetyl Glutamyl Heptapeptide-3) is an 8-amino acid synthetic biomimetic peptide (Ac-Glu-Glu-Met-Gln-Arg-Arg-Ala-Asp-NH2) developed by Lipotec S.A. (acquired by Lubrizol 2012) as a topical alternative to botulinum neurotoxin. Structural elongation of Argireline (Ac-EEMQRR-NH2) with two additional C-terminal residues (Ala-Asp) conferring ~30% greater anti-wrinkle activity. N-terminal acetyl cap and C-terminal amide enhance metabolic stability and reduce aminopeptidase/carboxypeptidase degradation. Amphiphilic character (two Glu, one Asp, two Arg residues) influences solubility and membrane interaction. Named for biomimetic relationship with SNAP-25 (Synaptosomal Associated Protein of 25 kDa), critical component of SNARE complex (Soluble N-ethylmaleimide-sensitive factor Attachment protein REceptor) responsible for calcium-dependent vesicle fusion and neurotransmitter release. Acts as biomimetic fragment of N-terminal SNARE motif of SNAP-25, competitively inhibiting endogenous SNAP-25 incorporation into ternary SNARE complex (VAMP/synaptobrevin, syntaxin-1, SNAP-25). At 1.5 mM achieves ~43% inhibition of glutamate release in vitro (Errante 2020). Partial, dose-dependent, reversible modulation produces muscle relaxation (not paralysis) - fundamentally distinct from botulinum toxin type A which enzymatically cleaves SNAP-25 causing complete irreversible blockade. Synergistic with Leuphasyl (Pentapeptide-18): 0.75 mM SNAP-8 alone = 38% inhibition, Leuphasyl alone = 7%, combined = 47% (exceeds additive, independent mechanisms). Hydrophilic character (LogP <0) presents stratum corneum permeation challenge, driving research into microneedle patches, liposomal encapsulation, penetration enhancers. Stable pH 4.0-7.0, lyophilized form stable at -20°C, oxidation-sensitive methionine at position 3.
Mechanism of Action
SNAP-8 exerts effects through multiple mechanisms: (1) SNARE Complex Competitive Inhibition - acts as biomimetic fragment of N-terminal SNARE motif of SNAP-25 (Synaptosomal Associated Protein 25 kDa); competitively inhibits endogenous SNAP-25 incorporation into ternary SNARE complex consisting of VAMP/synaptobrevin (vesicle membrane), syntaxin-1 (plasma membrane), and SNAP-25 (plasma membrane-associated); SNARE proteins assemble into coiled-coil four-helix bundle functioning as molecular "zipper" that draws vesicle and plasma membranes into proximity for membrane fusion and neurotransmitter exocytosis; at 1.5 mM concentration achieves ~43% inhibition of glutamate release in vitro (Errante 2020); partial, dose-dependent inhibition produces muscle relaxation rather than paralysis; (2) Neuromuscular Junction Modulation - reduces efficiency of acetylcholine exocytosis via SNARE complex modulation at neuromuscular junction; attenuates strength and frequency of facial muscle contractions without eliminating them; particularly relevant for expression lines where repeated contraction contributes to wrinkle formation; Apland 2003 demonstrated truncated SNAP-25 products inhibited depolarization-dependent glutamate release from hippocampal cultures and depressed synaptic transmission in Aplysia buccal ganglion cells; (3) Reversible Modulation - fundamentally distinct from botulinum toxin type A which enzymatically cleaves SNAP-25 via zinc-dependent metalloprotease activity causing complete, irreversible blockade lasting 3-6 months; SNAP-8 provides graded, titratable response proportional to concentration, reversible upon treatment cessation; (4) Synergistic Interaction with Leuphasyl - at equimolar 0.75 mM: SNAP-8 alone = 38% inhibition, Leuphasyl alone = 7%, combined = 47% (exceeds additive prediction); synergy arises from independent mechanisms: SNAP-8 targets SNARE complex assembly (presynaptic vesicle fusion machinery), Leuphasyl operates through opioid receptor-mediated presynaptic inhibition (enkephalin-mimetic); (5) Structural Basis - N-terminal acetyl cap and C-terminal amide enhance metabolic stability, reduce aminopeptidase/carboxypeptidase degradation; amphiphilic character from two Glu, one Asp, two Arg residues influences solubility and membrane interaction; single Met at position 3 confers oxidation sensitivity (methionine sulfoxide byproduct reduces activity).
“The combination provides synergistic effects on metabolic parameters by targeting both hypothalamic and peripheral pancreatic pathways.”
Preclinical Research Summary
Blanes-Mira et al. (2002, Int J Cosmet Sci): established foundational mechanism for SNAP-25 mimetic peptides; hexapeptide Ac-EEMQRR-NH2 (Argireline) inhibited calcium-dependent catecholamine release from permeabilized chromaffin cells by interfering with SNARE complex formation. Errante et al. (2020, Biomolecules): at 1.5 mM SNAP-8 achieved ~43% inhibition of glutamate release in vitro; demonstrated synergistic activity with Leuphasyl (0.75 mM SNAP-8 alone = 38%, Leuphasyl alone = 7%, combined = 47%). Apland et al. (2003, Toxicology): truncated SNAP-25 products inhibited depolarization-dependent glutamate release from hippocampal cultures and depressed synaptic transmission in Aplysia buccal ganglion cells. Lee et al. (2019, Ann Dermatol): elastase inhibitory activity and anti-wrinkle effect correlate to SNAP-8 concentration; demonstrates collagen/elastin protective mechanisms beyond SNARE inhibition. Zhang et al. (2023, J Anal Sci Technol): LC-MS/MS method development for SNAP-8 quantification; retention time 4.76 min, LOD 0.0018 μg/mL, LOQ 0.0036 μg/mL. Barros et al. (2022, Front Chem): SNAP-8-loaded polymeric nanoparticles with chitosan coating demonstrated sustained release profile, improved skin permeation, non-cytotoxic to HaCaT cells. Pharmacokinetics: hydrophilic character (LogP <0) presents stratum corneum permeation barrier; topically applied with minimal systemic absorption; reversible effects upon treatment cessation. Stability: optimal pH 4.0-7.0, lyophilized form stable at -20°C, oxidation-sensitive methionine at position 3 requires protection from light, moisture, oxidizing agents. Comparative mechanism: botulinum toxin type A cleaves SNAP-25 via metalloprotease causing complete irreversible blockade lasting 3-6 months with paralysis; SNAP-8 competitively inhibits SNAP-25 incorporation providing partial, dose-dependent, reversible relaxation without paralysis.
Academic References
1. Blanes-Mira C, et al. (2002). A synthetic hexapeptide (Argireline) with antiwrinkle activity. Int J Cosmet Sci. 24(5):303-310. doi:10.1046/j.1467-2494.2002.00153.x [Foundational mechanism: Ac-EEMQRR-NH2 inhibits SNARE complex]
2. Errante F, et al. (2020). Cosmeceutical Peptides in the Framework of Sustainable Wellness Economy. Biomolecules. 10(7):1056. doi:10.3390/biom10071056 [SNAP-8: 43% glutamate release inhibition at 1.5mM, synergistic with Leuphasyl]
3. Apland JP, et al. (2003). Inhibition of neurotransmitter release by peptides that mimic the N-terminal domain of SNAP-25. Toxicology. 190(3):251-261. doi:10.1016/s0300-483x(03)00172-9 [Truncated SNAP-25 products inhibit glutamate release, depress synaptic transmission]
4. Lee SH, et al. (2019). Elastase Inhibitory Activity and Antiwrinkle Effect of Cosmetics Containing Saussurea Involucrata Extract. Ann Dermatol. 31(Suppl):S29-S33. doi:10.5021/ad.2019.31.S.S29 [SNAP-8 concentration-dependent elastase inhibition, collagen/elastin protection]
5. Zhang W, et al. (2023). Quantitative analysis of acetyl octapeptide-3 in cosmetics using liquid chromatography-tandem mass spectrometry. J Anal Sci Technol. 14:25. doi:10.1186/s40543-023-00392-3 [LC-MS/MS method: RT 4.76 min, LOD 0.0018 μg/mL]
6. Barros RC, et al. (2022). Acetyl Octapeptide-3-Loaded Polymeric Nanoparticles: Proof of Concept of Topical Application. Front Chem. 10:833141. doi:10.3389/fchem.2022.833141 [Chitosan-coated nanoparticles: sustained release, improved permeation, non-cytotoxic]
7. Wang Y, et al. (2013). Effect of Argireline on ASICs and MMPs: new insight into the anti-wrinkle mechanism of anti-aging cosmetics. Int J Cosmet Sci. 35(6):621-628. doi:10.1111/ics.12087 [Argireline (hexapeptide precursor) mechanism review]
8. Maia Campos PM, et al. (2014). Skin moisturizing effects of peptides: a comparative study. Int J Cosmet Sci. 36(5):434-439. doi:10.1111/ics.12141 [Peptide moisturizing mechanisms in cosmeceutical applications]
9. Lupo MP, Cole AL. (2007). Cosmeceutical peptides. Dermatol Ther. 20(5):343-349. doi:10.1111/j.1529-8019.2007.00148.x [Comprehensive review of cosmeceutical peptides including SNAP-8]
10. Jahn R, Scheller RH. (2006). SNAREs--engines for membrane fusion. Nat Rev Mol Cell Biol. 7(9):631-643. doi:10.1038/nrm2002 [Comprehensive SNARE complex molecular biology review]