SNAP-8
An acetylated octapeptide investigated as a SNARE-complex / SNAP-25 mimetic in cosmetic-science and neuroexocytosis mechanistic research.
Molecular Profile
- Type
- Synthetic octapeptide (8 amino acids)
- Molecular formula
- C42H72N16O15S
- Molecular weight
- 1073.2 g/mol
- CAS number
- 868844-74-0
- Amino acids
- 8
- Sequence
- Ac-Glu-Glu-Met-Gln-Arg-Arg-Ala-Asp-NH2
- Modification
- N-terminal acetylation and C-terminal amidation (reduces amino- and carboxypeptidase susceptibility); two-residue Ala-Asp extension of the parent six-residue Acetyl Hexapeptide-8 scaffold.
Mechanism & Target Class
SNAP-8 is designed to mimic the N-terminal region of SNAP-25, a component of the ternary SNARE complex (SNAP-25 / syntaxin / VAMP-synaptobrevin) that drives Ca²⁺-dependent synaptic vesicle fusion and neurotransmitter exocytosis. By competing with native SNAP-25 for incorporation into SNARE complex formation, the peptide is proposed to modulate vesicle docking and neurotransmitter release — a mechanism of competitive interference at the protein-assembly level, distinct from proteolytic cleavage mechanisms. The two-residue extension over the parent hexapeptide covers a larger portion of the SNAP-25 N-terminal helical segment, which structural studies identify as critical for SNARE complex assembly. Computational work additionally implicates synaptotagmin-1 (the Ca²⁺ sensor for exocytosis) as a potential secondary interaction site for this peptide class.
Storage & Handling
- Lyophilized
- -20°C, sealed, protected from light and moisture; ~24 months.
- Handling
- Methionine residue is oxidation-sensitive — protect from light and oxygen; avoid freeze-thaw cycles; keep sealed.
Primary Database
References (22)
Reviews
1Khvotchev M, Soloviev M. (2022). Biomolecules
- 2
Errante F, Ledwoń P, Latajka R, Rovero P, Papini AM. (2020). Frontiers in Chemistry
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Jahn R, Fasshauer D. (2012). Nature
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Zdrada-Nowak J, Surgiel-Gemza A, Szatkowska M. (2025). Int J Mol Sci
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Pintea A, Manea A, Pintea C, Vlad RA, Bîrsan M, Antonoaea P, Rédai EM, Ciurba A. (2025). Biomolecules
- 6
Rizo J, Xu J. (2015). Annu Rev Biophys
Clinical
7Shin et al. (2024). Annals of Dermatology
- 8
Xing M, Liu H, Meng F, Ma Y, Zhang S, Gao Y. (2022). Polymers (Basel)
- 9
Avcil M, Akman G, Klokkers J, Jeong D, Çelik A. (2020). Journal of Cosmetic Dermatology
Primary research
10Baglamis S, Feyzioglu-Demir E, Akgol S. (2023). Polymer Bulletin
- 11
Ji M, et al. (2020). Journal of Analytical Science and Technology
- 12
Wongrattanakamon P, Nimmanpipug P, Sirithunyalug B, Jiranusornkul S. (2018). Molecular and Cellular Biochemistry
- 13
Lim SH, Sun Y, Thiruvallur Madanagopal T, Rosa V, Kang L. (2018). Scientific Reports
- 14
Blanes-Mira C, Merino JM, Valera E, Fernandez-Ballester G, Gutierrez LM, Viniegra S, Perez-Paya E, Ferrer-Montiel A. (2004). Journal of Neurochemistry
- 15
Blanes-Mira C, et al. (2002). Int J Cosmet Sci
- 16
Apland JP, Biser JA, Adler M, Ferrer-Montiel AV, Montal M, Canaves JM, Filbert MG. (1999). Journal of Applied Toxicology
DOI: 10.1002/(SICI)1099-1263(199912)19:1+<S23::AID-JAT609>3.0.CO;2-X
- 17
Ferrer-Montiel AV, Gutierrez LM, Apland JP, Canaves JM, Gil A, Viniegra S, Biser JA, Adler M, Montal M. (1998). FEBS Letters
- 18
Gutierrez LM, Viniegra S, Rueda J, Ferrer-Montiel AV, Canaves JM, Montal M. (1997). Journal of Biological Chemistry
- 19
Gutierrez LM, Canaves JM, Ferrer-Montiel AV, Reig JA, Montal M, Viniegra S. (1995). FEBS Letters
- 20
Blanes-Mira C, Pastor MT, Valera E, Fernández-Ballester G, Merino JM, Gutierrez LM, Perez-Payá E, Ferrer-Montiel A. (2003). Biochemical Journal
- 21
Ramakrishnan S, Bera M, Coleman J, Rothman JE, Krishnakumar SS. (2020). eLife
- 22
Pozzi D, Corradini I, Matteoli M. (2019). Neuroscience
