Selank Atomized Solution 30ml

What is Selank?

Selank is a laboratory-developed compound modeled after the naturally occurring peptide tuftsin (Thr–Lys–Pro–Arg–Pro–Gly–Pro). Research investigations indicate that it influences GABA-related neural activity and alters gene expression involved in neuropeptide communication. Its proposed biological actions include effects on BDNF regulation, inflammatory signaling such as IL-6, and pathways involved in monoamine processing, which has led to scientific interest in its potential role within neuroimmune regulatory mechanisms.

Why is Selank studied?

Selank is a synthetic heptapeptide: the immunoactive tetrapeptide tuftsin (Thr-Lys-Pro-Arg) extended with Pro-Gly-Pro. The extension is a stability device — it slows enzymatic cleavage of a sequence that is otherwise degraded very quickly — and it is the reason the analogue, rather than tuftsin, is the material used in laboratory work.⁴

How is Selank studied in the lab?

• Research findings indicate that Selank modulates several intracellular signaling routes involved in GABA-related neurotransmission, regulation of monoamine systems, and immune-associated transcriptional activity. Studies in animal models have associated Selank administration with changes in gene expression influencing receptor-mediated signaling, enzymatic processing pathways, and cytokine-driven intercellular communication.
• Additional investigations have examined Selank’s influence on enkephalinase activity, suggesting a possible indirect effect on the regulation of endogenous peptide metabolism and receptor–ligand dynamics at the molecular scale.

What has preclinical research reported?

Selank is commonly employed in laboratory and preclinical settings to study how short regulatory peptides influence cellular signaling processes. Typical areas of investigation include:

• Profiling changes in gene expression associated with neurotransmitter-related systems
• Examining elements of GABA-related signaling in rodent brain tissue
• Assessing the activity of enzymes involved in enkephalin metabolism through biochemical testing
• Studying immune-associated transcriptional responses, including cytokine and chemokine regulation
• Analyzing peptide stability and receptor-linked signaling behavior under experimental conditions

Forms studied and handling

The material is supplied as a lyophilized (freeze-dried) powder. Freeze-drying is used for peptides because removing water suppresses the hydrolysis and aggregation routes that dominate degradation in solution, and the resulting amorphous solid is far more stable on storage than the corresponding liquid.⁵ Reported degradation routes for peptides in the solid state include deamidation of asparagine and glutamine residues, oxidation of methionine and tryptophan, and physical aggregation, all of which are accelerated by residual moisture, elevated temperature and repeated freeze-thaw cycling.⁶ Sealed vials are therefore held at −20 °C, protected from light, and reconstituted material is kept cold and used within a short working window. For laboratory research use only.

References

1. Volkova, A., Shadrina, M., Kolomin, T., Andreeva, L., Limborska, S., Myasoedov, N., & Slominsky, P. (2016). Selank Administration Affects the Expression of Some Genes Involved in GABAergic Neurotransmission. Frontiers in pharmacology, 7, 31. https://doi.org/10.3389/fphar.2016.00031. PMID 26924987
2. Semenova TP, Kozlovskaya MM, Zakharova NM, Kozlovskii II, Zuikov AV. Effect of selank on cognitive processes after damage inflicted to the cerebral catecholamine system during early ontogeny. Bull Exp Biol Med. 2007;144(5):689-691. doi:10.1007/s10517-007-0406-2. PMID 18683497
3. Kolomin T, Shadrina M, Andreeva L, Slominsky P, Limborska S, Myasoedov N. Expression of inflammation-related genes in mouse spleen under tuftsin analog Selank. Regul Pept. 2011;170(1-3):18-23. doi:10.1016/j.regpep.2011.05.001. PMID 21609736
4. Kolomin T, Shadrina M, Andreeva L, et al. Expression of inflammation-related genes in mouse spleen under tuftsin analog Selank. Regulatory Peptides. 2011;170(1-3):18-23. doi:10.1016/j.regpep.2011.05.001
5. Wang W. Lyophilization and development of solid protein pharmaceuticals. International Journal of Pharmaceutics. 2000;203(1-2):1-60. doi:10.1016/S0378-5173(00)00423-3
6. Manning MC, Chou DK, Murphy BM, et al. Stability of protein pharmaceuticals: an update. Pharmaceutical Research. 2010;27(4):544-575. doi:10.1007/s11095-009-0045-6