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SNAP-8
$70.00
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SNAP-8
Overview
SNAP-8, also known as Acetyl Glutamyl Heptapeptide-1 or Acetyl Octapeptide-3, is a synthetic octapeptide developed as a topical neuromodulatory ingredient and elongated analog of Argireline (Acetyl Hexapeptide-3). It is designed to reduce the appearance of dynamic facial expression lines through competitive inhibition of the SNARE complex. It is not intended for injection and is used primarily in topical cosmeceutical formulations.
Mechanism of Action
SNAP-8 mimics the N-terminal end of SNAP-25, a key component of the SNARE (SNapREceptor) protein complex responsible for synaptic vesicle fusion and neurotransmitter release. By competing with SNAP-25 for a position in the SNARE complex, SNAP-8 partially destabilizes the complex, reducing acetylcholine release at the neuromuscular junction and attenuating the intensity of facial muscle contractions. This mechanism is pharmacologically analogous to botulinum toxin but operates via competitive inhibition rather than enzymatic cleavage.
Research and Clinical Data
Manufacturer-funded in vivo studies using 10% SNAP-8 in topical formulations demonstrated up to 63% reduction in wrinkle depth around the eye area after 28 days of twice-daily application. Independent research reports more conservative improvements of 10–20%. SNAP-8 is reported to be approximately 30% more active than Argireline in both in vitro and in vivo testing.
Administration
Applied topically at concentrations of 3–10% in serums, creams, and other emulsion formulations. Twice-daily application is recommended; consistent use over 4–8 weeks is required to observe measurable improvements. Effects are not permanent and diminish upon discontinuation.
Potential Adverse Effects
Considered generally safe and well tolerated in clinical testing over 12 weeks. No significant adverse events reported at recommended concentrations. Some formulations may cause mild irritation in sensitive skin types.
Properties
1. Basic Information
2. Structural Properties Peptide Nature: Linear octapeptide with N-terminal acetylation and C-terminal amidation; sequence corresponds to residues 12–19 of the native SNAP-25 protein N-terminal domain, extended by two residues relative to Argireline (Acetyl Hexapeptide-3)
Secondary Structure: Largely unstructured in free solution; proposed to adopt a transient extended conformation that mimics the SNAP-25 N-terminal helix upon SNARE complex interaction; molecular dynamics studies suggest conformational flexibility enables competitive insertion into the SNARE bundle assembly site
Hydrophobicity: Predominantly hydrophilic; charged glutamate, arginine, and aspartate residues dominate the polarity profile; methionine residue introduces a minor hydrophobic contribution
Charge: Net negative to neutral charge at physiological pH; two glutamate (pKa ~4.1) and one aspartate (pKa ~3.9) residues offset by two arginine residues (pKa ~12.5); overall charge profile slightly negative at pH 7.4
3. Solubility
4. Stability Thermal Stability: Stable in formulated aqueous systems at typical cosmetic processing temperatures (up to 40°C); avoid prolonged exposure above 50°C during formulation
Proteolytic Stability: N-terminal acetylation and C-terminal amidation confer resistance to exopeptidase degradation at both termini; susceptible to endopeptidase activity in biological matrices; stability in topical formulations is generally considered adequate for cosmetic applications
Storage: Store lyophilized at −20°C or 2–8°C protected from light; aqueous solutions stable at 2–8°C for up to 30 days; formulated products stable according to individual formulation pH and preservative system
5. Chemical Reactivity N-terminal acetylation blocks the free amine; reduces potential for Maillard reaction with reducing sugars in complex formulations
Methionine residue (Met-3 in sequence) is susceptible to oxidation to methionine sulfoxide under oxidative conditions; antioxidant co-formulation is recommended for long-term stability
Glutamate and aspartate residues contribute to pH-dependent solubility and charge; formulation pH 4.5–7.0 is recommended for optimal stability
No disulfide bonds; oxidative stability is favorable relative to cysteine-containing peptides
C-terminal amidation prevents carboxypeptidase degradation and contributes to in-formulation stability
6. Other Properties
- Name: SNAP-8 (Acetyl Glutamyl Heptapeptide-1; Acetyl Octapeptide-3)
- Type: Synthetic acetylated octapeptide; SNARE complex competitive inhibitor
- Length: 8 amino acids
- Sequence: Ac-Glu-Glu-Met-Gln-Arg-Arg-Ala-Asp-NH₂ (acetylated N-terminus, amidated C-terminus)
- Molecular Weight: ~1,075 Da
- Formula: C₄₄H₇₃N₁₅O₁₇S
2. Structural Properties Peptide Nature: Linear octapeptide with N-terminal acetylation and C-terminal amidation; sequence corresponds to residues 12–19 of the native SNAP-25 protein N-terminal domain, extended by two residues relative to Argireline (Acetyl Hexapeptide-3)
Secondary Structure: Largely unstructured in free solution; proposed to adopt a transient extended conformation that mimics the SNAP-25 N-terminal helix upon SNARE complex interaction; molecular dynamics studies suggest conformational flexibility enables competitive insertion into the SNARE bundle assembly site
Hydrophobicity: Predominantly hydrophilic; charged glutamate, arginine, and aspartate residues dominate the polarity profile; methionine residue introduces a minor hydrophobic contribution
Charge: Net negative to neutral charge at physiological pH; two glutamate (pKa ~4.1) and one aspartate (pKa ~3.9) residues offset by two arginine residues (pKa ~12.5); overall charge profile slightly negative at pH 7.4
3. Solubility
- Highly soluble in water and aqueous buffers; solubility exceeds 20 mg/mL in sterile water
- Compatible with standard cosmetic aqueous vehicles including hydrogels, serums, and emulsions at working concentrations of 3–10%
- Supplied as lyophilized white powder; reconstitution in water recommended prior to formulation incorporation
4. Stability Thermal Stability: Stable in formulated aqueous systems at typical cosmetic processing temperatures (up to 40°C); avoid prolonged exposure above 50°C during formulation
Proteolytic Stability: N-terminal acetylation and C-terminal amidation confer resistance to exopeptidase degradation at both termini; susceptible to endopeptidase activity in biological matrices; stability in topical formulations is generally considered adequate for cosmetic applications
Storage: Store lyophilized at −20°C or 2–8°C protected from light; aqueous solutions stable at 2–8°C for up to 30 days; formulated products stable according to individual formulation pH and preservative system
5. Chemical Reactivity N-terminal acetylation blocks the free amine; reduces potential for Maillard reaction with reducing sugars in complex formulations
Methionine residue (Met-3 in sequence) is susceptible to oxidation to methionine sulfoxide under oxidative conditions; antioxidant co-formulation is recommended for long-term stability
Glutamate and aspartate residues contribute to pH-dependent solubility and charge; formulation pH 4.5–7.0 is recommended for optimal stability
No disulfide bonds; oxidative stability is favorable relative to cysteine-containing peptides
C-terminal amidation prevents carboxypeptidase degradation and contributes to in-formulation stability
6. Other Properties
- SNARE mimicry: Sequence corresponds to the N-terminal SNAP-25 domain region involved in SNARE complex nucleation; competitive displacement of native SNAP-25 is the proposed mechanism in biochemical assay literature
- Potency relative to Argireline: SNAP-8 is reported as approximately 30% more active than Argireline (Acetyl Hexapeptide-3) in comparative in vitro SNARE assembly inhibition assays; attributed to the two additional residues extending the competitive binding interface
- Topical application context: Designed for transdermal delivery in cosmeceutical formulations; percutaneous absorption studies report limited but measurable dermal penetration at standard cosmetic concentrations
- Non-toxic profile: Cytotoxicity studies report no significant adverse cell viability effects at concentrations up to 10% in standard keratinocyte and fibroblast cell culture models
Description
SNAP-8 is a synthetic research peptide and has been described in the scientific literature as an acetylated octapeptide analog of the N-terminal sequence of SNAP-25, a component of the SNARE (SNapREceptor) protein complex. Publications referencing SNAP-8 discuss it in the context of synaptic vesicle fusion pharmacology, neuromuscular junction signaling, and SNARE complex interaction dynamics within experimental systems.
Reports involving SNAP-8 describe its proposed competitive interaction with SNARE complex assembly and associated downstream signaling properties under defined experimental conditions. Observations of SNARE complex destabilization markers, acetylcholine release-associated signaling components, and neuromuscular junction activity are limited to non-clinical research settings and are reported as descriptive findings within cellular and biochemical model studies.
All references to SNAP-8 are confined to mechanistic and observational research contexts and do not extend beyond laboratory-based investigation.
In the scientific literature, SNAP-8 has been referenced in non-clinical research involving SNARE complex binding assays, neuromuscular signaling studies, and topical delivery model investigations. These publications describe experimental contexts in which molecular interactions, protein complex assembly markers, and pathway-associated signaling components were observed and recorded.
Reported research contexts include examination of:
- SNARE complex assembly dynamics and competitive binding interaction patterns observed in biochemical model systems
- SNAP-25 N-terminal sequence mimicry and associated protein–protein interaction markers evaluated in experimental settings
- Acetylcholine release-associated neuromuscular junction signaling components assessed under experimental conditions
- Topical delivery and percutaneous absorption dynamics reported in formulation research contexts
- Comparative SNARE inhibition profiles relative to Argireline (Acetyl Hexapeptide-3) in experimental systems
All reported applications are confined to descriptive investigation within controlled laboratory research environments.
Mechanistic discussions in preclinical publications describe SNAP-8 as an octapeptide in which N-terminal acetylation and sequence elongation relative to Argireline are described as contributing to enhanced competitive displacement of native SNAP-25 within the SNARE complex assembly pathway. This mechanism is described as pharmacologically analogous to botulinum toxin in its proposed site of action, but operating via reversible competitive inhibition rather than enzymatic cleavage. These descriptions are limited to molecular and biochemical observations within experimental systems and do not imply functional outcomes beyond the reported research context.
SNAP-8 is supplied as a research-grade peptide material. Identity and composition have been reported as characterized using analytical techniques commonly applied to peptide research materials, including chromatographic and mass spectrometric methods. Individual laboratories determine handling, storage, and analytical verification parameters in accordance with internal research protocols.
COA
Storage
All of our products are manufactured using the Lyophilization (Freeze Drying) process, which ensures that our products remain 100% stable for shipping for up to 3-4 months. Once the peptides are reconstituted (mixed with bacteriostatic water), they must be stored in the fridge to maintain stability. After reconstitution, the peptides will remain stable for up to 30 days.
Lyophilization is a unique dehydration process, also known as cryodesiccation, where the peptides are frozen and then subjected to low pressure. This causes the water in the peptide vial to sublimate directly from solid to gas, leaving behind a stable, crystalline white structure known as lyophilized peptide. The puffy white powder can be stored at room temperature until you're ready to reconstitute it with bacteriostatic water.
Once peptides have been received, it is imperative that they are kept cold and away from light. If the peptides will be used immediately, or in the next several days, weeks or months, short-term refrigeration under 4°C (39°F) is generally acceptable. Lyophilized peptides are usually stable at room temperatures for several weeks or more, so if they will be utilized within weeks or months such storage is typically adequate.
For longer term storage (several months to years) it is more preferable to store peptides in a freezer at -80°C (-112°F). When storing peptides for months or even years, freezing is optimal in order to preserve the peptide's stability.
Lyophilization is a unique dehydration process, also known as cryodesiccation, where the peptides are frozen and then subjected to low pressure. This causes the water in the peptide vial to sublimate directly from solid to gas, leaving behind a stable, crystalline white structure known as lyophilized peptide. The puffy white powder can be stored at room temperature until you're ready to reconstitute it with bacteriostatic water.
Once peptides have been received, it is imperative that they are kept cold and away from light. If the peptides will be used immediately, or in the next several days, weeks or months, short-term refrigeration under 4°C (39°F) is generally acceptable. Lyophilized peptides are usually stable at room temperatures for several weeks or more, so if they will be utilized within weeks or months such storage is typically adequate.
For longer term storage (several months to years) it is more preferable to store peptides in a freezer at -80°C (-112°F). When storing peptides for months or even years, freezing is optimal in order to preserve the peptide's stability.
