Selank / Semax

A research-use-only two-component blend of two synthetic heptapeptides, each a short N-terminal sequence extended with a C-terminal Pro-Gly-Pro (glyproline) tripeptide that confers protease resistance.

Molecular Profile

Type
Peptide blend

Components

Selank

Molecular formula
C33H57N11O9
Molecular weight
~751.9 g/mol
CAS number
129954-34-3
Sequence
Thr-Lys-Pro-Arg-Pro-Gly-Pro (TKPRPGP)

Semax

Molecular formula
C37H51N9O10S
Molecular weight
~813.9 g/mol
CAS number
80714-61-0
Sequence
Met-Glu-His-Phe-Pro-Gly-Pro (MEHFPGP)

Mechanism & Target Class

Both peptides belong to the 'glyproline-stabilized' class: a short N-terminal sequence is extended with a C-terminal Pro-Gly-Pro (PGP) tripeptide that slows proteolysis. Selank corresponds structurally to the tetrapeptide tuftsin sequence (Thr-Lys-Pro-Arg) carrying the C-terminal PGP extension, giving the heptapeptide Thr-Lys-Pro-Arg-Pro-Gly-Pro. Semax is a synthetic peptide corresponding to the ACTH(4-7) sequence (Met-Glu-His-Phe) carrying the same C-terminal PGP extension, giving the heptapeptide Met-Glu-His-Phe-Pro-Gly-Pro; its N-terminal methionine residue is susceptible to oxidation. The shared PGP scaffold is the common structural feature characterized across both molecules, and the C-terminal glyproline motif is described in the chemistry literature as the modification that resists enzymatic degradation.

Storage & Handling

Lyophilized
Store frozen and protected from light and moisture; commonly handled at -20°C for long-term storage as a sealed lyophilized powder.
Handling
The C-terminal Pro-Gly-Pro motif confers resistance to enzymatic degradation; nonetheless, reconstituted solutions are less stable than the lyophilate. The methionine residue in Semax is susceptible to oxidation — protect from light and air. Avoid repeated freeze-thaw cycles. For research use only; not for human or veterinary use.

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