Snap-8

SNAP-8 Peptide Overview

SNAP-8 (Acetyl Octapeptide-3) is a sophisticated, laboratory-engineered octapeptide designed as a higher-potency evolution of the hexapeptide Acetyl Hexapeptide-8. This peptide is composed of a specific sequence of eight amino acids: Acetyl-Glu-Glu-Met-Gln-Arg-Arg-Ala-Asp. In biochemical research, SNAP-8 is studied for its unique ability to mimic the N-terminal end of SNAP-25, a protein essential for the formation of the SNARE (SNARE protein complex) system.

The synthesis of SNAP-8 concludes with a high-precision lyophilization (freeze-drying) process, resulting in a polymorphous crystalline powder. This physical state may show minor variations in crystal density or localized aggregation; however, these are purely structural characteristics and do not impact the chemical purity or potency of the peptide. Comprehensive analytical testing confirms that the product maintains exceptional uniformity across all batches.

SNAP-8 is primarily utilized in research environments focusing on neuromuscular signaling and dermal mechanobiology. Researchers analyze its role in regulating cellular tension and the behavior of elastic networks within the skin. Additional investigations focus on how the peptide modulates expression patterns linked to stress responses and the long-term structural integrity of tissue systems.

SNAP-8 Product Structure

The molecular architecture of SNAP-8 is defined by its linear chain of amino acids, modified at the N-terminus to enhance stability and lipophilicity.

Chemical Structure Formula:

Acetyl-Glutamyl-Glutamyl-Methionyl-Glutaminyl-Arginyl-Arginyl-Alanyl-Aspartic Acid

Structural Profile Table:

Property

Specification

Product Name

SNAP-8 Peptide

INCI Name

Acetyl Glutamyl Heptapeptide-1

IUPAC Name

Acetyl-L-alpha-glutamyl-L-alpha-glutamyl-L-methionyl-L-glutaminyl-L-arginyl-L-arginyl-L-alanyl-L-aspartic acid

Molecular Sequence

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

Appearance

White crystalline lyophilized powder

Solubility

Highly soluble in water and aqueous buffers

Purity (HPLC)

Minimum 98.0%

SNAP-8 Research and Mechanism of Action

SNAP-8 functions as a structural analogue of the SNAP-25 protein. In physiological systems, the SNARE complex is a "molecular hook" that allows neurotransmitter vesicles to fuse with the cell membrane, releasing signals that trigger muscle contraction. SNAP-8 competes with SNAP-25 for a position in this complex.

When SNAP-8 is incorporated into the SNARE complex instead of the natural protein, the complex becomes slightly destabilized. This destabilization reduces the efficiency of neurotransmitter release (exocytosis). Consequently, the signal for muscle contraction is attenuated. In dermal research, this mechanism is explored for its ability to reduce the depth of wrinkles caused by repetitive facial expressions, particularly in the forehead and periorbital (eye) areas.

Key Research Objectives:

• Neuromodulation: Assessing the inhibition of catecholamine release in cell models.
• Dermal Signaling: Observing changes in mechanical tension within skin tissue equivalents.
• Comparative Efficacy: Evaluating SNAP-8 as a topical, non-invasive alternative to Botulinum Toxin.

Scientific Authors and Acknowledgments

Article Author

This review was compiled, organized, and edited by Dr. Carlos Blanes-Mira, Ph.D. Dr. Blanes-Mira is a distinguished biochemist recognized for his innovative work in peptide research, specifically focusing on neurotransmitter-inhibiting sequences. His scientific contributions have been fundamental in advancing the understanding of peptide analogues that interact with the SNARE protein complex and influence neuromuscular communication.

Scientific Journal Authors

Dr. Carlos Blanes-Mira, along with co-authors J. Clemente, G. Jodas, A. Gil, G. Fernandez-Ballester, B. Ponsati, L. Gutierrez, E. Perez-Paya, and A. Ferrer-Montiel, conducted the seminal studies on SNAP-8. Their work demonstrated how SNAP-8 interferes with SNARE complex formation, thereby modulating neurotransmitter release.

Further research by Y. Wang, N. Cirillo, A. Carruthers, and J. Yong has expanded these findings, examining how SNAP-family peptides influence dermal mechanics and cellular responses. These investigations provide the scientific basis for the role of SNAP peptides in modern dermatological research. This acknowledgment credits their scientific efforts and does not imply an endorsement of this specific product.

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

Long-Term Stability

All SNAP-8 products are produced via lyophilization, which allows for stability during transit for 3 to 4 months at ambient temperatures. However, for long-term preservation of the peptide's structural integrity, the following protocols are recommended:

• Lyophilized Powder: Store at 4 degrees Celsius (39 degrees Fahrenheit) for up to 12 months. For storage exceeding one year, keep at -20 degrees Celsius or -80 degrees Celsius to prevent degradation.
• Reconstituted Solution: Once the peptide is dissolved in a sterile buffer or bacteriostatic water, it must be refrigerated at 4 degrees Celsius. Use within 30 days for optimal results.

Best Practices to Prevent Degradation

• Avoid Freeze-Thaw Cycles: Repeated temperature fluctuations can break peptide bonds. Aliquot the peptide into smaller single-use volumes before freezing.
• Moisture Control: Lyophilized peptides are hygroscopic. Always allow vials to reach room temperature before opening to prevent atmospheric moisture from condensing on the powder.
• Light Sensitivity: Store in dark vials or keep in a light-shielded environment to prevent photo-oxidation.
• Atmospheric Protection: For sensitive residues, sealing vials under an inert gas like Nitrogen or Argon can further extend shelf life.