N-Acetyl Semax
An N-terminally acetylated, C-terminally amidated synthetic heptapeptide analog of Semax, retaining the ACTH(4–7) core sequence with a Pro-Gly-Pro C-terminal extension.
Quick answers
What is N-Acetyl Semax?
N-Acetyl Semax is an N-terminally acetylated, C-terminally amidated synthetic heptapeptide analog of Semax, retaining the ACTH(4–7) core sequence with a Pro-Gly-Pro C-terminal extension. It is a synthetic linear heptapeptide derivative (N-terminal acetylation, C-terminal amidation); structural analog of ACTH(4–10) of 7 amino acids with a molecular weight of 855.0 g/mol and the formula C39H54N10O10S.
How much published research cites N-Acetyl Semax?
The Luvaminos N-Acetyl Semax record cites 20 published references, dated 2001 to 2025. Each is listed on this page with a link to its source.
Does Luvaminos test N-Acetyl Semax, and where is the certificate?
Luvaminos does not currently stock N-Acetyl Semax. Every peptide lot Luvaminos sells is tested by Freedom Diagnostics Testing, PLLC, an independent laboratory, and its certificate is published at luvaminos.com/coa under the lot number printed on the vial.
What modifications does N-Acetyl Semax carry?
N-Acetyl Semax: N-terminal acetylation and C-terminal amidation of the parent Semax heptapeptide (CAS 80714-61-0); these terminal modifications are the defining structural difference from the parent.
How is N-Acetyl Semax powder stored?
Sealed N-Acetyl Semax powder: -20°C, protected from light and moisture; stable long term as lyophilized powder. N-terminal acetylation and C-terminal amidation are structural features studied for resistance to terminal exopeptidase cleavage relative to the parent peptide. As with other methionine-containing peptides, protect from oxidizing conditions and avoid repeated freeze-thaw cycles.
How is N-Acetyl Semax different from Semax?
N-Acetyl Semax and Semax are different compounds: N-Acetyl Semax has 7 amino acids, a molecular weight of 855.0 g/mol and formula C39H54N10O10S; Semax has 7 amino acids, a molecular weight of 813.93 g/mol and formula C37H51N9O10S. N-Acetyl Semax: N-terminal acetylation and C-terminal amidation of the parent Semax heptapeptide (CAS 80714-61-0). Semax: C-terminal Pro-Gly-Pro tripeptide extension of the ACTH(4-7) core.
How is N-Acetyl Semax different from Adamax?
N-Acetyl Semax and Adamax are different compounds: N-Acetyl Semax has 7 amino acids, a molecular weight of 855.0 g/mol and formula C39H54N10O10S; Adamax has 9 amino acids, a molecular weight of 984.10 g/mol and formula C44H61N11O13S. N-Acetyl Semax: N-terminal acetylation and C-terminal amidation of the parent Semax heptapeptide (CAS 80714-61-0). Adamax: N-terminal acetylation.
Molecular Profile
- Type
- Synthetic linear heptapeptide derivative (N-terminal acetylation, C-terminal amidation); structural analog of ACTH(4–10)
- Molecular formula
- C39H54N10O10S
- Molecular weight
- 855.0 g/mol
- CAS number
- 2920938-90-3
- Amino acids
- 7
- Sequence
- Ac-Met-Glu-His-Phe-Pro-Gly-Pro-NH₂ (acetyl-MEHFPGP-amide)
- Modification
- N-terminal acetylation and C-terminal amidation of the parent Semax heptapeptide (CAS 80714-61-0); these terminal modifications are the defining structural difference from the parent.
Mechanism & Target Class
N-Acetyl Semax retains the ACTH(4–7) core sequence (Met-Glu-His-Phe) of the parent Semax heptapeptide. The Pro-Gly-Pro C-terminal extension found in the parent confers resistance to carboxypeptidase cleavage. The additional N-terminal acetyl group and C-terminal amide are structural modifications studied for resistance to terminal exopeptidase attack (Shevchenko et al., 2013). Structural chemistry work (Magrì et al., 2016) characterized how N-terminal acetylation alters the copper(II) and zinc(II) coordination geometry of the peptide and examined associated in-vitro properties. Studies of the parent compound used tritium-labeled peptide to characterize specific, reversible, calcium-dependent binding sites in rat basal forebrain membranes. The histidine-containing sequence coordinates Cu(II) and Zn(II) ions, situating it in bioinorganic research contexts.
Storage & Handling
- Lyophilized
- -20°C, protected from light and moisture; stable long term as lyophilized powder.
- Handling
- N-terminal acetylation and C-terminal amidation are structural features studied for resistance to terminal exopeptidase cleavage relative to the parent peptide. As with other methionine-containing peptides, protect from oxidizing conditions and avoid repeated freeze-thaw cycles.
Primary Database
References (20)
Reviews
1Dergunova LV, Filippenkov IB, Limborska SA, Myasoedov NF (2023). Genes (Basel)
Clinical
2Gusev EI, Martynov MYu, Kostenko EV, Petrova LV, Bobyreva SN (2018). Zh Nevrol Psikhiatr Im SS Korsakova
Primary research
3Liu R, Chen Y, Huang H, et al. (2025). British Journal of Pharmacology
- 4
Tomasello MF, Di Rosa MC, Naletova I, et al. (2025). Bioinorganic Chemistry and Applications
- 5
Radchenko AI, Kuzubova EV, Apostol AA, et al. (2025). Acta Naturae
- 6
Inozemtseva LS, Yatsenko KA, Glazova NYu, et al. (2024). European Journal of Pharmacology
- 7
Sciacca MFM, et al. (2022). ACS Chemical Neuroscience
- 8
Dergunova LV, Dmitrieva VG, Filippenkov IB, et al. (2021). Molecular Biology (Moscow)
- 9
Sudarkina OY, Filippenkov IB, Stavchansky VV, et al. (2021). International Journal of Molecular Sciences
- 10
Filippenkov IB, Stavchansky VV, Denisova AE, et al. (2020). Genes (Basel)
- 11
Medvedeva EV, Dmitrieva VG, Limborska SA, Myasoedov NF, Dergunova LV (2017). Molecular Genetics and Genomics
- 12
Magrì A, Tabbì G, Giuffrida A, et al. (2016). Journal of Inorganic Biochemistry
- 13
Medvedeva EV, Dmitrieva VG, Povarova OV, et al. (2014). BMC Genomics
- 14
Shevchenko KV, Nagaev IY, Andreeva LA, Shevchenko VP, Myasoedov NF (2013). Doklady Biological Sciences
- 15
Shadrina M, Kolomin T, Agapova T, et al. (2010). Journal of Molecular Neuroscience
- 16
Dmitrieva VG, Povarova OV, Skvortsova VI, Limborska SA, Myasoedov NF, Dergunova LV (2010). Cellular and Molecular Neurobiology
- 17
Dolotov OV, Karpenko EA, Inozemtseva LS, et al. (2006). Brain Research
- 18
Dolotov OV, Karpenko EA, Seredenina TS, et al. (2006). Journal of Neurochemistry
- 19
Eremin KO, Kudrin VS, Saransaari P, et al. (2005). Neurochemical Research
- 20
Shadrina MI, Dolotov OV, Grivennikov IA, et al. (2001). Neuroscience Letters
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