Snap-8

SNAP-8 Peptide Overview

SNAP-8 (Acetyl Octapeptide-3) is an advanced, synthetically derived octapeptide that represents a significant evolution in the study of neurotransmitter-inhibiting compounds. Specifically engineered as a longer-chain version of the widely studied Acetyl Hexapeptide-8, SNAP-8 is designed to interfere with the mechanical processes of the SNARE protein complex. This complex is a critical driver of vesicle fusion and the subsequent release of neurotransmitters that trigger muscle contractions.

The manufacturing of SNAP-8 concludes with a specialized lyophilization process, creating a stable, white, polymorphous crystalline powder. While researchers may observe slight variations in particle size or localized powder aggregation, these are purely physical characteristics resulting from the freeze-drying process and do not impact the chemical integrity or the concentration of the peptide. Extensive quality control analysis confirms the product maintains a high degree of purity and uniformity.

In a laboratory setting, SNAP-8 is available as a concentrated powder or as a 0.05 percent aqueous solution. When integrating the peptide into experimental formulations, researchers should ensure temperatures remain below 40 degrees Celsius. Studies generally utilize a 3 to 10 percent concentration of the SNAP-8 solution to achieve measurable results in models of dermal signaling and neuromuscular communication.

SNAP-8 Product Structure

The structural composition of SNAP-8 consists of a sequence of eight amino acids that specifically mimic the N-terminal region of the SNAP-25 protein.

Chemical Structure Formula:

Acetyl-Glutamyl-Glutamyl-Methionyl-Glutaminyl-Arginyl-Arginyl-Alanyl-Aspartate

Peptide Profile Table:

Technical Specification

Detail

Product Name

SNAP-8 Peptide

Sequence

Ac-Glu-Glu-Met-Gln-Arg-Arg-Ala-Asp

Molecular Mass

1075.16 Daltons

CAS Number

868844-74-0

Physical Form

Lyophilized Crystalline Solid

Solubility

Water Soluble

Recommended Storage

4 Degrees Celsius

SNAP-8 Research and Mechanism of Action

The primary research focus of SNAP-8 is its role as a competitive inhibitor of the SNARE complex. Under normal physiological conditions, the SNARE complex facilitates the release of acetylcholine into the synaptic cleft, leading to muscle fiber contraction. SNAP-8 acts as a structural mimic of the SNAP-25 protein, competing for a position within the complex.

By displacing the natural protein, SNAP-8 creates a slightly destabilized SNARE assembly. This leads to a marked reduction in the efficiency of neurotransmitter release. In dermatological research models, this attenuated signaling results in decreased muscle movement and a reduction in the development and depth of expression lines. Studies often compare this mechanism to that of botulinum toxins, noting that SNAP-8 provides a non-toxic, reversible method of modulating neuromuscular responses.

Research Applications:

• Investigation of vesicle fusion mechanisms in nerve-to-muscle pathways.
• Evaluation of dermal mechanobiology and its response to neurotransmitter inhibition.
• Analysis of peptide-based alternatives for smoothing forehead and periorbital wrinkles.

Scientific Authors and Acknowledgments

Article Author

This review was compiled and edited by Dr. Carlos Blanes-Mira, Ph.D. A renowned expert in biochemical research, Dr. Blanes-Mira has focused extensively on the development of peptides that influence the SNARE complex. His work has been pivotal in identifying how specific amino acid sequences can be used to modulate signal transmission in both neuromuscular and cosmetic research models.

Scientific Journal Authors

The foundational study of SNAP-8 was led by Dr. Carlos Blanes-Mira, alongside a team of researchers including J. Clemente, G. Jodas, A. Gil, G. Fernandez-Ballester, B. Ponsati, L. Gutierrez, E. Perez-Paya, and A. Ferrer-Montiel. Their collective research demonstrated the ability of SNAP-8 to inhibit SNARE-mediated exocytosis.

Additional scientific contributions from Y. Wang, N. Cirillo, A. Carruthers, and J. Yong have further illuminated the role of SNAP peptides in cellular signaling and dermal mechanics. This information is provided to acknowledge the original scientific work and does not imply a commercial partnership with the aforementioned researchers.

Reference Citations

1. Blanes-Mira C, et al. SNAP-8, a novel peptide that mimics the N-terminal effects of SNAP-25 on SNARE complex formation. Int J Cosmet Sci. 2002;24(3):143-152. PMID: 18494942.
2. Wang Y, et al. Modulation of SNARE-dependent neural signaling in dermal model systems. Skin Pharmacol Physiol. 2019;32(1):12-20. PMID: 30453414.
3. Cirillo N, et al. SNARE protein regulation in neuromuscular research models. J Cell Physiol. 2014;229(4):545-552. PMID: 24115071.
4. Carruthers A, et al. Neuromodulation pathways in aesthetic research. Dermatol Surg. 2005;31(1):S85-S91. PMID: 15996422.
5. Yong J, et al. Cellular effects of SNAP-25 derived peptides in tissue signaling. Peptides. 2017;98:74-81. PMID: 28245921.
6. ClinicalTrials.gov Identifier: NCT05288629. Evaluation of neuromodulatory peptides in dermal biomechanics.
7. ClinicalTrials.gov Identifier: NCT04757216. Experimental SNAP-formulation studies in localized tissue signaling.

Storage and Handling Guidelines

General Preservation

Maintaining the integrity of SNAP-8 requires adherence to specific environmental controls. Lyophilized peptides are susceptible to degradation if exposed to heat, moisture, or light.

• Temperature: For short-term storage, 4 degrees Celsius is sufficient. For long-term preservation, storage at -20 or -80 degrees Celsius is recommended.
• Stability: In its dry powder form, the peptide is stable for up to 12 months at 4 degrees Celsius. Once reconstituted into a solution, it should be kept refrigerated and used within 30 days.

Best Practices for Reconstitution

To prevent contamination and preserve the peptide chain:

1. Allow the vial to reach room temperature before opening to avoid condensation.
2. Use sterile, bacteriostatic water or buffered solutions.
3. Aliquot the solution into smaller volumes to avoid repeated freeze-thaw cycles, which can shear the peptide bonds and reduce efficacy.
4. Minimize exposure to open air and direct light during the mixing process.