{"id":2248,"date":"2026-06-27T19:42:13","date_gmt":"2026-06-27T19:42:13","guid":{"rendered":"https:\/\/one-peptides.com\/?post_type=product&p=2248"},"modified":"2026-10-05T13:49:43","modified_gmt":"2026-10-05T13:49:43","slug":"selank-spray-10mg","status":"publish","type":"product","link":"https:\/\/one-peptides.com\/es\/producto\/selank-spray-10mg\/","title":{"rendered":"Selank Spray 10 mg"},"content":{"rendered":"

One-Peptides SELANK 10 mg \u2014 tuftsin analogue nasal spray for laboratory research<\/h2>\n

This product is a reagent intended solely for scientific research (Research Use Only, RUO) conducted under laboratory conditions. It is not a medicinal product, dietary supplement, cosmetic or medical device. It is not intended for consumption or for administration to humans or animals outside a strictly controlled, legally compliant research protocol. The material holds no registration authorising it for diagnostic or therapeutic applications. Responsibility for the lawful storage, handling and use of the reagent rests with the research facility.<\/em><\/p>\n

Selank derives from the same scientific tradition as the better-known Semax \u2014 the Russian school of regulatory peptidology, which from the 1980s onwards developed the idea of rationally modifying short fragments of endogenous proteins. The starting point here was tuftsin: a natural tetrapeptide derived from the Fc portion of immunoglobulin G, described as an immune-modulating factor. A team from the Institute of Molecular Genetics of the Russian Academy of Sciences took this sequence and extended it with a stabilising motif, obtaining a heptapeptide with considerably greater stability in the biological environment. This is how Selank<\/a> arose \u2014 a molecule studied by Russian scientists in the anxiolytic, nootropic and immunomodulatory context.<\/p>\n

One-Peptides offers Selank as a pre-dissolved solution in a nasal spray, with a content of 10 mg, as a research material of purity confirmed by HPLC.<\/strong> The choice of this format is not accidental. Selank is a centrally acting peptide, and in the Russian literature it was studied precisely in the form of drops and spray for intranasal administration \u2014 a route that has long interested neuroscience as a way of transporting molecules along the nose-to-brain axis. Below we present an honest picture of what is known about Selank from the literature, drawing a clear distinction between the data from studies and the status of the reagent, and noting that a substantial part of the available work comes from Russian literature with limited independent replication.<\/p>\n

Selank is a synthetic heptapeptide built from seven amino acid residues with the sequence Thr-Lys-Pro-Arg-Pro-Gly-Pro and a molecular mass of approximately 751 Da. It is an analogue of tuftsin \u2014 a natural fragment of an immunoglobulin \u2014 extended at the C-terminus with a Pro-Gly-Pro sequence that protects against enzymatic degradation. It was developed at the Institute of Molecular Genetics of the Russian Academy of Sciences; in the literature it is analysed in the anxiolytic and nootropic context, as well as in relation to modulation of the GABA and monoamine systems and to immunomodulation.<\/strong><\/p>\n

What Selank is \u2014 sequence and class<\/h2>\n

Selank belongs to the group of synthetic regulatory peptides designed as stable analogues of natural endogenous molecules. Its prototype is tuftsin \u2014 a tetrapeptide with the sequence Thr-Lys-Pro-Arg, excised from the Fc portion of immunoglobulin G and described in the literature as a factor with immunomodulatory properties. The problem with tuftsin from a research perspective was its rapid degradation, which is why the Russian team extended the sequence with a C-terminal Pro-Gly-Pro motif. The result is a heptapeptide with the sequence Thr-Lys-Pro-Arg-Pro-Gly-Pro, considerably more resistant to the action of aminopeptidases and carboxypeptidases.<\/p>\n

The same design solution recurs in the related Semax (Met-Glu-His-Phe-Pro-Gly-Pro) \u2014 the proline residues adjacent to glycine form a structural anchor that hinders cleavage by proteolytic enzymes in serum and nervous tissue. This recurring Pro-Gly-Pro motif has become a hallmark of the Russian school of regulatory peptidology. Although Selank and Semax derive from different prototypes \u2014 the first from tuftsin, the second from a fragment of ACTH \u2014 they share the same design philosophy: take a short fragment of an endogenous protein, retain its active core and add anti-degradation protection.<\/p>\n

Chemical characterisation<\/h3>\n\n\n\n\n\n\n\n\n\n\n\n
Parameter<\/th>\nValue<\/th>\n<\/tr>\n<\/thead>\n
Class<\/td>\nHeptapeptide, synthetic tuftsin analogue<\/td>\n<\/tr>\n
Sequence<\/td>\nThr-Lys-Pro-Arg-Pro-Gly-Pro (TKPRPGP)<\/td>\n<\/tr>\n
Molecular mass<\/td>\n~751 Da<\/td>\n<\/tr>\n
Form<\/td>\nPre-dissolved solution, nasal spray<\/td>\n<\/tr>\n
Content<\/td>\n10 mg<\/td>\n<\/tr>\n
Purity<\/td>\nHPLC \u226598%<\/td>\n<\/tr>\n
Identity confirmation<\/td>\nMass spectrometry (MS)<\/td>\n<\/tr>\n<\/tbody>\n<\/table>\n

The sequence Thr-Lys-Pro-Arg-Pro-Gly-Pro is rich in proline residues, which gives the peptide a more rigid conformation and limits the number of sites susceptible to enzymatic cleavage. The N-terminal fragment Thr-Lys-Pro-Arg corresponds to the tuftsin sequence and constitutes the core to which the biological activity of the molecule has been linked in the literature. Its small mass, approximately 751 Da, places Selank in the group of small peptides \u2014 a feature of relevance from the perspective of research into transport across biological barriers.<\/p>\n

Mechanism of action in research<\/h2>\n

The mechanism of action of Selank has been described in the literature as pleiotropic \u2014 the peptide was analysed in relation to its effect on several signalling systems in parallel, without a single, isolated target receptor. The picture below stems from preclinical work, in large part from Russian literature.<\/p>\n