SNAP-8
SNAP-8, chemically known as Acetyl Glutamyl Heptapeptide-3 or Acetyl Octapeptide-3, is a synthetic octapeptide developed as a functional fragment and analogue of Argireline® (Acetyl Hexapeptide-8). It was designed to mimic the N-terminal end of SNAP-25, a key protein involved in neurotransmitter vesicle release, and to modulate the SNARE complex formation that mediates synaptic vesicle fusion.
Through this mechanism, SNAP-8 is widely used in research studying neuromuscular transmission, neuropeptide signaling, and synaptic exocytosis inhibition.
In biochemical and cosmetic research models, it has been shown to attenuate catecholamine release, reduce mechanical tension at neuromuscular junctions, and modulate facial muscle contraction signaling — earning it the reputation as a “neuropeptide complex modulator” in peptide science.
As a research compound, SNAP-8 is often used to explore peptidic inhibitors of neurotransmitter release, botulinum-toxin–mimetic mechanisms, and muscle cell response modulation in vitro.
Price range: $20.00 through $25.00
Structural Highlights:
- Derived Sequence: Modeled on the N-terminal domain of the SNAP-25 (synaptosomal-associated protein 25 kDa), a critical component of the SNARE complex responsible for vesicular fusion.
- Mechanism-Specific Design: Functions as a competitive inhibitor for SNAP-25 assembly, disrupting the formation of the SNARE complex required for neurotransmitter release.
- Terminal Modifications:
- N-terminal acetylation increases peptide stability and membrane permeability.
- C-terminal amidation enhances resistance to enzymatic degradation and improves receptor binding affinity.
- Structure-Function Balance: Optimized for receptor mimicry while maintaining conformational stability in aqueous environments.
SNAP-8 is primarily studied in cellular and molecular neuroscience, cosmeceutical peptide research, and neuromuscular modulation models.
Its structural design and inhibitory behavior make it a valuable tool for studying synaptic transmission, neurotoxin alternatives, and peptide-based exocytosis inhibitors.
SCIENTIFIC STRUCTURE & MOLECULAR DESIGN
- Inhibits SNARE complex formation (syntaxin, SNAP-25, and synaptobrevin), reducing neurotransmitter release at the presynaptic cleft.
- Mimics the mechanism of botulinum toxin type A at the molecular level, providing a non-enzymatic model for neuromuscular relaxation research.
- Enables studies of vesicle-fusion dynamics, exocytosis inhibition, and neuropeptide interference mechanisms.
POTENTIAL BENEFITS
- Modulates neuropeptide-dependent signaling pathways in vitro.
- Reduces acetylcholine release in cultured neuron or muscle cell models, aiding in the study of synaptic signaling attenuation.
- Serves as a probe for neurochemical plasticity and neuro-exocytosis regulation.
Peptide Stability & Structure-Activity Relationships
- Exhibits high chemical stability due to acetylation and amidation at both termini.
- Used in comparative studies alongside Argireline® (Ac-Hexapeptide-8) to analyze the effect of chain length and residue variation on SNARE complex binding affinity.
- Enables evaluation of structure-activity relationships (SAR) in neuropeptidic inhibitor design.
Dermatological and Cellular Stress Models
- In cell-culture models, SNAP-8 has been shown to reduce catecholamine-induced contraction, supporting research into anti-stress and neuromuscular tension responses.
- Frequently studied in combination with GHK-Cu and Matrixyl® peptides to assess synergistic ECM and neurochemical regulation.
This product is supplied strictly for laboratory research use only. It is not a drug, food, or cosmetic and must not be administered to humans or animals. Proper handling procedures and safety protocols should be followed by trained professionals when working with this material.
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Disclaimer: For Research Use Only
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