ADAMAX Reference
Reviewed by Dr. Martina Rossi, PhD
Scientific Contributor and Reviewer · Reviewed
Molecular Profile
Compound
ADAMAX
CAS number
N/A (novel research peptide)
Molecular formula
C50H69N11O11S
Molecular weight
1032.24 g/mol
Amino acid sequence
Met-Glu-His-Phe-Pro-Gly-Pro, acetyl-capped at one end and carrying an adamantylglycine unit at the other, from the product page prose
Purity
greater than 99 percent
Physical form
Lyophilized powder
What ADAMAX is, structurally
ADAMAX is a seven-residue peptide carrying a group at each end: an acetyl cap on one and a single adamantylglycine unit on the other. The product page states the sequence, Met-Glu-His-Phe-Pro-Gly-Pro.
That core is worth recognizing, because it is the same seven residues as Semax, a separate product sold here. Semax is C37H51N9O10S at 813.92; this compound is C50H69N11O11S at 1032.24. Subtracting one from the other leaves C13H18N2O, a difference of 218.30, which is what the two capping groups contribute. Same core, different ends, and a mass gap no analysis would blur.
The adamantyl unit should dominate the handling. Adamantane is a rigid, cage-shaped hydrocarbon and markedly lipophilic, and attaching one to a molecule of only a thousand daltons shifts its whole character rather than modifying it slightly. On that reasoning this should behave closer to a lipidated peptide than an ordinary short one, though no measurement on this compound has been published.
The acetyl cap has a separate consequence. Blocking the N-terminus removes the free alpha-amino group, so Edman degradation cannot sequence this peptide directly, and identity has to be established by other means such as mass spectrometry and NMR.
Two other features follow from the sequence. The single methionine is the one oxidation-prone residue: it goes first to the sulfoxide, adding sixteen units, and on to the sulfone, adding thirty-two, under stronger or longer oxidation; there is no cysteine, so no disulfide chemistry. The two prolines make the backbone unusually rigid, since proline's ring restricts rotation, and each proline amide can sit cis or trans, so slow interconversion between those forms can broaden or split chromatographic peaks.
Structure at a glance
ADAMAX: C 50, N 11, O 11, S 1.
Drawn from the product database.
Reconstitution and handling
Sterile water alone may not be sufficient. The adamantyl group is strongly lipophilic and can dominate the solubility of a molecule this size, so a vial that resists water is behaving as its structure predicts rather than indicating a fault. The conventional approach is to dissolve in a small volume of a water-miscible solvent such as DMSO or ethanol, then dilute into aqueous buffer with mixing.
Add diluent slowly down the inside wall of the vial and swirl gently. Do not vortex; a partly lipophilic molecule is surface-active enough to foam.
Adsorptive loss deserves more attention than on an ordinary short peptide. Lipophilic groups partition onto surfaces, so losses to both plastic and glass are worth allowing for at low concentration, and minimizing transfers helps more than changing tube type.
No reducing agent is needed. The single sulfur is a methionine thioether and there is no disulfide to protect.
This is laboratory preparation chemistry, not dosing, administration, or protocol guidance of any kind.
Storage and stability
Store the lyophilized powder at -20 degrees C, sealed, desiccated and protected from light, and let a cold vial warm before opening. Reconstituted, hold at 2 to 8 degrees C, or aliquot and freeze rather than thawing repeatedly.
Methionine oxidation is the principal named liability, adding sixteen units as the sulfoxide, and air, warmth and light all accelerate it. A sealed, cold, dark vial is the control.
The glutamate carries the ordinary isomerization liability, and both prolines make the neighbouring bonds slower to hydrolyze than most, which works in the material's favor. There is no asparagine or glutamine in the stated sequence, so classical deamidation has no site to act on here, which is a definite statement rather than an inference because the sequence is known.
Reconstituted solutions of a partly lipophilic molecule deserve a shorter working life than the chemistry alone would suggest, since the physical state is less stable and material can come out of solution on cooling.
These are storage conditions for the material, not dosing or administration guidance.
How ADAMAX is tested
Reversed-phase HPLC establishes chromatographic purity as area percent, and this molecule sits at the retentive end of the range. The adamantyl group binds a C18 surface strongly, so a higher organic proportion is needed than for an ordinary heptapeptide, and a gradient designed for short polar peptides may not elute it within the run.
Detection is available near 214 nm, and the phenylalanine gives some absorbance near 260 nm, though histidine and phenylalanine together make a weaker chromophore than tryptophan or tyrosine would. There is neither of the latter in the sequence.
Area percent is a chromatographic measure and not peptide content by weight. Solid-phase synthesis delivers a salt, and residual trifluoroacetate is its own impurity class.
Mass spectrometry confirms identity against 1032.24. A result sixteen units high indicates methionine sulfoxide. A result near 813.9 would indicate the uncapped core rather than a light impurity, which is a separate product on this site.
These describe general methodology, not a claim about any particular batch.
Handling FAQ
Why will this not dissolve as readily as a peptide of its size should?+−
Because of the adamantyl group. Adamantane is a rigid lipophilic cage, and on a molecule of about a thousand daltons it substantially governs solubility. A water-miscible co-solvent followed by dilution into buffer is the conventional approach.
How is this distinguished from Semax?+−
By mass, easily. The two share the same seven-residue core, but this compound carries two capping groups that Semax does not, worth 218.30 together. Semax is 813.92 and this is 1032.24, a gap no analysis would blur. Full specifications for ADAMAX.

Reviewed for scientific accuracy
Dr. Martina Rossi, PhD
PhD, Université Grenoble Alpes · Scientific Contributor and Reviewer
Dr. Rossi's doctoral research at Université Grenoble Alpes examined the vascular functions of bone morphogenetic proteins. Her peer-reviewed work spans cell and molecular biology, vascular biology, and gene therapy, in journals including Cardiovascular Research, Scientific Reports, and Brain Sciences. She reviews Pure Peptides' product, reference, and research pages for scientific accuracy against the sources they cite.
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