Adamax
A synthetic Semax analogue: the N-acetylated Semax sequence extended by Ala-Gly to nine residues, ending in a free carboxylic acid (984.1 g/mol).
View Adamax in the storeQuick answers
What is Adamax?
Adamax is a synthetic Semax analogue: the N-acetylated Semax sequence extended by Ala-Gly to nine residues, ending in a free carboxylic acid (984.1 g/mol). It is a synthetic peptide (Semax analogue, 9 residues) with a molecular weight of 984.10 g/mol and the formula C44H61N11O13S.
How much published research cites Adamax?
The Luvaminos Adamax record cites 22 published references, dated 2001 to 2025. Each is listed on this page with a link to its source.
Does Luvaminos test Adamax, and where is the certificate?
Yes. Every Adamax lot Luvaminos sells is tested by Freedom Diagnostics Testing, PLLC, an independent laboratory. The current 10 mg lot, ADA-10-001, measured 99.81% purity by HPLC and a net content of 11.29 mg, tested October 15, 2026. Its certificate is published at luvaminos.com/coa/ADA-10-001.
What modifications does Adamax carry?
Adamax: N-terminal acetylation; an Ala-Gly extension after the Semax sequence; a free C-terminal carboxylic acid.
How is Adamax powder stored?
Sealed Adamax powder: Store refrigerated or at −20 °C, protected from light; use desiccant as needed. Avoid repeated freeze-thaw cycles; protect from light and microbial contamination.
How is Adamax different from Semax?
Adamax and Semax are different compounds: Adamax has 9 amino acids, a molecular weight of 984.10 g/mol and formula C44H61N11O13S; Semax has 7 amino acids, a molecular weight of 813.93 g/mol and formula C37H51N9O10S. Adamax: N-terminal acetylation. Semax: C-terminal Pro-Gly-Pro tripeptide extension of the ACTH(4-7) core.
How is Adamax different from N-Acetyl Semax?
Adamax and N-Acetyl Semax are different compounds: Adamax has 9 amino acids, a molecular weight of 984.10 g/mol and formula C44H61N11O13S; N-Acetyl Semax has 7 amino acids, a molecular weight of 855.0 g/mol and formula C39H54N10O10S. Adamax: N-terminal acetylation. N-Acetyl Semax: N-terminal acetylation and C-terminal amidation of the parent Semax heptapeptide (CAS 80714-61-0).
Molecular Profile
- Type
- Synthetic peptide (Semax analogue, 9 residues)
- Molecular formula
- C44H61N11O13S
- Molecular weight
- 984.10 g/mol
- Amino acids
- 9
- Sequence
- Ac-Met-Glu-His-Phe-Pro-Gly-Pro-Ala-Gly-OH
- Modification
- N-terminal acetylation; an Ala-Gly extension after the Semax sequence; a free C-terminal carboxylic acid.
Mechanism & Target Class
A synthetic peptide built on the Semax sequence (Met-Glu-His-Phe-Pro-Gly-Pro), itself an analogue of the ACTH(4–10) fragment. The N-terminus is acetylated and the chain is extended by Ala-Gly, ending in a free carboxylic acid. N-terminal acetylation and C-terminal extension are modifications studied in peptide analogues for their effect on resistance to enzymatic degradation. Its molecular weight is 984.1 g/mol (monoisotopic mass 983.42 Da).
Storage & Handling
- Lyophilized
- Store refrigerated or at −20 °C, protected from light; use desiccant as needed.
- Handling
- Avoid repeated freeze-thaw cycles; protect from light and microbial contamination.
References (22)
Reviews
1Markov DD, Dolotov OV, Grivennikov IA (2023). Int. J. Mol. Sci.
Primary research
2Li B, et al. (2010). FEBS Lett
- 3
Dolotov OV, et al. (2006). Brain Res
- 4
Radchenko AI, Sobolevsky OI, et al. (2025). Acta Naturae
- 5
Sciacca MFM, Naletova I, Giuffrida ML, Attanasio F (2022). ACS Chem. Neurosci.
- 6
Sudarkina OY, Remizova JA, et al. (2021). Int. J. Mol. Sci.
- 7
Dolotov OV, Karpenko EA, Seredenina TS, et al. (2006). J. Neurochem.
- 8
Medvedeva EM, Dergunova LV, Filippenkov IB, et al. (2014). BMC Genomics
- 9
Dolotov OV, Karpenko EA, Inozemtseva LS, et al. (2006). Brain Res.
- 10
Shadrina MI, Dolotov OV, Grivennikov IA, et al. (2001). Neurosci. Lett.
- 11
Agapova TY, Agniullin YV, Shadrina MI, et al. (2007). Neurosci. Lett.
- 12
Shadrina M, Kolomin T, Agapova T, et al. (2009). J. Mol. Neurosci.
- 13
Storozhevykh TP, Tukhbatova GR, Senilova YE, et al. (2007). Bull. Exp. Biol. Med.
- 14
Grivennikov IA, Dolotov OV, Zolotarev YA, et al. (2008). Restor. Neurol. Neurosci.
- 15
Eremin KO, Kudrin VS, Saransaari P, et al. (2005). Neurochem. Res.
- 16
Bashkatova VG, Koshelev VB, Fadyukova OE, et al. (2001). Brain Res.
- 17
Dmitrieva VG, Kolomin TA, Shadrina MI, et al. (2009). Cell Mol. Neurobiol.
- 18
Medvedeva EV, Dmitrieva VG, Limborska SA, et al. (2017). Mol. Genet. Genomics
- 19
Filippenkov IB, Stavchansky VV, Denisova AE, et al. (2020). Genes
- 20
Dergunova LV, Filippenkov IB, Stavchansky VV, et al. (2021). Mol. Biol.
- 21
Stavchansky VV, Yuzhakov VV, Sevan'kaeva LE, et al. (2024). Curr. Issues Mol. Biol.
- 22
Filippenkov IB, Shpetko YY, Stavchansky VV, et al. (2024). Biomedicines
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