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

PubChem CID 71587832

References (22)

  1. Reviews

    1

    Khvotchev M, Soloviev M. (2022). Biomolecules

    DOI: 10.3390/biom12121779PubMed 36551207

  2. 2

    Errante F, Ledwoń P, Latajka R, Rovero P, Papini AM. (2020). Frontiers in Chemistry

    DOI: 10.3389/fchem.2020.572923PubMed 33195061

  3. 3

    Jahn R, Fasshauer D. (2012). Nature

    DOI: 10.1038/nature11320PubMed 23060190

  4. 4

    Zdrada-Nowak J, Surgiel-Gemza A, Szatkowska M. (2025). Int J Mol Sci

    DOI: 10.3390/ijms26125722PubMed 40565185

  5. 5

    Pintea A, Manea A, Pintea C, Vlad RA, Bîrsan M, Antonoaea P, Rédai EM, Ciurba A. (2025). Biomolecules

    DOI: 10.3390/biom15010088PubMed 39858482

  6. 6

    Rizo J, Xu J. (2015). Annu Rev Biophys

    DOI: 10.1146/annurev-biophys-060414-034057PubMed 26098518

  7. Clinical

    7

    Shin et al. (2024). Annals of Dermatology

    DOI: 10.5021/ad.23.136

  8. 8

    Xing M, Liu H, Meng F, Ma Y, Zhang S, Gao Y. (2022). Polymers (Basel)

    DOI: 10.3390/polym14214475PubMed 36365468

  9. 9

    Avcil M, Akman G, Klokkers J, Jeong D, Çelik A. (2020). Journal of Cosmetic Dermatology

    DOI: 10.1111/jocd.13009PubMed 31134751

  10. Primary research

    10

    Baglamis S, Feyzioglu-Demir E, Akgol S. (2023). Polymer Bulletin

    DOI: 10.1007/s00289-022-04663-8

  11. 11

    Ji M, et al. (2020). Journal of Analytical Science and Technology

    DOI: 10.1186/s40543-020-00232-8

  12. 12

    Wongrattanakamon P, Nimmanpipug P, Sirithunyalug B, Jiranusornkul S. (2018). Molecular and Cellular Biochemistry

    DOI: 10.1007/s11010-017-3196-5PubMed 29019108

  13. 13

    Lim SH, Sun Y, Thiruvallur Madanagopal T, Rosa V, Kang L. (2018). Scientific Reports

    DOI: 10.1038/s41598-017-18454-zPubMed 29371611

  14. 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

    DOI: 10.1046/j.1471-4159.2003.02133.xPubMed 14675156

  15. 15

    Blanes-Mira C, et al. (2002). Int J Cosmet Sci

    DOI: 10.1046/j.1467-2494.2002.00153.xPubMed 18498523

  16. 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. 17

    Ferrer-Montiel AV, Gutierrez LM, Apland JP, Canaves JM, Gil A, Viniegra S, Biser JA, Adler M, Montal M. (1998). FEBS Letters

    DOI: 10.1016/s0014-5793(98)01012-6PubMed 9755864

  18. 18

    Gutierrez LM, Viniegra S, Rueda J, Ferrer-Montiel AV, Canaves JM, Montal M. (1997). Journal of Biological Chemistry

    DOI: 10.1074/jbc.272.5.2634PubMed 9006897

  19. 19

    Gutierrez LM, Canaves JM, Ferrer-Montiel AV, Reig JA, Montal M, Viniegra S. (1995). FEBS Letters

    DOI: 10.1016/0014-5793(95)00944-5

  20. 20

    Blanes-Mira C, Pastor MT, Valera E, Fernández-Ballester G, Merino JM, Gutierrez LM, Perez-Payá E, Ferrer-Montiel A. (2003). Biochemical Journal

    DOI: 10.1042/BJ20030509PubMed 12852787

  21. 21

    Ramakrishnan S, Bera M, Coleman J, Rothman JE, Krishnakumar SS. (2020). eLife

    DOI: 10.7554/eLife.54506PubMed 32401194

  22. 22

    Pozzi D, Corradini I, Matteoli M. (2019). Neuroscience

    DOI: 10.1016/j.neuroscience.2018.11.009PubMed 30476527