Selank 10mg

Selank is a synthetic peptide analog of the natural human protein tuftsin, designed exclusively for in vitro laboratory research. Tuftsin, first identified at Tufts University in 1970, is a tetrapeptide derived from the Fc-domain of immunoglobulin (Ig) G.

It plays a significant role in immunomodulation by participating in antigen processing, the formation of reactive oxygen species, and the development of antigen complexes.^1,2 Selank mimics tuftsin but includes an additional three amino acids at the C-terminus (Pro-Gly-Pro), which enhances its stability for experimental research.

Development Background

Selank was developed at the Institute of Molecular Genetics of the Russian Academy of Sciences as a stabilized structural analog of tuftsin.

In Vitro Gene Expression Research

In vitro studies using IMR-32 cells, a human neuroblastoma cell line, examined the effects of Selank, GABA, and the antipsychotic drug olanzapine on the expression of genes involved in GABAergic neurotransmission.³

This cell-based approach allows researchers to study gene expression changes associated with GABAergic signaling in a controlled cell culture system, providing a basis for further research into Selank's molecular mechanisms at the cellular level.

Peptide Structure: The Pro-Gly-Pro Stabilizing Extension

Native tuftsin (Thr-Lys-Pro-Arg) is understood to have a very short plasma half-life due to rapid cleavage by aminopeptidases, since its free N-terminal threonine and C-terminal arginine are both readily accessible cleavage sites.

Researchers designing Selank appended a Pro-Gly-Pro tripeptide to the tuftsin C-terminus specifically to sterically hinder this enzymatic degradation, since proline residues are poorly accommodated by many aminopeptidases and carboxypeptidases. This extension is the structural basis researchers cite for Selank's improved in vitro stability relative to native tuftsin.

Analytical Purity Verification

Purity verification for Selank typically combines HPLC and mass spectrometry to confirm the correct 7-residue sequence and free carboxylic acid C-terminus.

Given Selank's proline-rich composition, three of its seven residues, researchers reviewing a certificate of analysis are encouraged to confirm resolution from closely related synthesis byproducts that can arise from incomplete coupling at proline residues, which are more sterically hindered during solid-phase synthesis than most other amino acids.

Storage and Handling in the Laboratory Setting

Lyophilized Selank is stored under sub-zero freezer conditions to preserve integrity between experimental sessions, with the powder kept away from direct light, consistent with standard handling practices for short synthetic research peptides.

Comparative Research Context: Selank and Semax

Selank is frequently studied alongside Semax, another heptapeptide developed by the same Russian research program and sharing the identical Pro-Gly-Pro C-terminal stabilizing motif, though built on a different N-terminal sequence derived from ACTH rather than tuftsin.

Researchers comparing these two peptides have used their shared stabilization strategy but distinct parent sequences to investigate how the same protective structural modification performs across different bioactive peptide scaffolds in cell-based laboratory research.

Important Safety Information

Selank is intended for laboratory research use only (in vitro). It is not approved for human consumption, medical treatment, or therapeutic use. All research involving this peptide must comply with laboratory safety protocols and be conducted by qualified personnel in controlled research settings only.

Product Information

• Form: Lyophilized white powder
• Intended Use: In vitro research only

References

1. Fridkin M, Najjar VA. Tuftsin: Its Chemistry, Biology, and Clinical Potential. Crit Rev Biochem Mol Biol. 1989;24:1-40.
2. Najjar VA. Tuftsin, a natural activator of phagocyte cells: An overview. Ann N Y Acad Sci. 1983:1-11.
3. Filatova E, Kasian A, Kolomin T, et al. GABA, Selank, and Olanzapine Affect the Expression of Genes Involved in GABAergic Neurotransmission in IMR-32 Cells. Front Pharmacol. 2017;8:89.