NA Selank 50 mg

This 50 mg vial of NA Selank is supplied as a higher-content format for extended-study research applications. NA Selank (N-acetyl Selank, Ac-Selank) is the N-terminally acetylated analog of Selank, the synthetic heptapeptide developed at the Institute of Molecular Genetics of the Russian Academy of Sciences and built on the tuftsin-derived core sequence Thr-Lys-Pro-Arg-Pro-Gly-Pro. By capping the free N-terminal amine of the threonine residue with an acetyl group, NA Selank preserves the parent sequence while modifying its enzymatic stability and side-chain interaction profile. It is classified as a chemically stabilized tuftsin-derived synthetic heptapeptide studied alongside native Selank in GABAergic, neuropeptidergic, and adaptive-signalling research models.

The mechanism of action of NA Selank follows the same conceptual framework as Selank, with several distinguishing features attributable to N-terminal acetylation. Capping the N-terminal amine removes a major substrate recognition site for plasma and brain aminopeptidases, which extends the functional half-life of the peptide in laboratory preparations relative to the parent compound. The modification also reshapes the local electrostatic and steric environment around the threonine and lysine residues, which research models indicate can modify the GABAergic-binding profile, the interaction with enkephalin-degrading enzymes, and the engagement with tuftsin-related immune signaling pathways. As with native Selank, NA Selank is investigated for its influence on T-helper cell cytokine balance, expression of brain-derived neurotrophic factor (BDNF), and downstream signaling cascades relevant to stress adaptation and neuro-immune communication.

Research interest in NA Selank peptide spans enzymatic stability and proteolytic-degradation profiling, comparative GABAergic and neuropeptidergic signaling versus native Selank, immune-modulatory cytokine signaling, and gene-expression profiling in central nervous system tissue. Transcriptomic work on the parent compound has shown that Selank administration affects the expression of genes involved in GABAergic neurotransmission in rodent brain tissue (Volkova et al., 2016, Frontiers in Pharmacology), and NA Selank is studied in parallel to characterize how N-terminal acetylation reshapes these molecular readouts. These findings position NA Selank as a research tool for dissecting how N-terminal chemistry influences tuftsin-derived peptide function in integrated neuro-immune research workflows.

The peptide is supplied as a lyophilized powder to ensure optimal stability during storage and handling.

The tuftsin-derived peptide family has been a focal point of neuropeptide and immunomodulatory research since the 1970s, when investigators characterized the natural tetrapeptide Tuftsin (Thr-Lys-Pro-Arg) as a regulator of macrophage and lymphocyte activity. Building on this framework, researchers at the Institute of Molecular Genetics of the Russian Academy of Sciences extended the Tuftsin sequence with a Pro-Gly-Pro tripeptide tail to develop Selank, a heptapeptide with improved metabolic stability and a broader research profile spanning GABAergic neurotransmission, neurotrophic factor expression, and immune signaling.

NA Selank was developed within the analog program associated with this peptide family, in which N-terminal modifications are used as a tool to probe the structural determinants of tuftsin-derived peptide function. Acetylation of the N-terminal threonine eliminates a primary aminopeptidase recognition site and modifies local interactions with binding partners. Comparative studies of Ac-Selank versus Selank have examined the resulting changes in enzymatic stability, GABAergic-binding chemistry, cytokine regulation, and gene-expression profiles in central nervous system tissue research models.

NA Selank occupies a defined position in the Pepcore tuftsin-analog research catalog as a chemically stabilized counterpart to native Selank. It is studied alongside Selank 10 mg and other neuropeptide research tools in laboratories investigating tuftsin-derived peptide chemistry, neuro-immune interactions, and the role of N-terminal modifications in heptapeptide function.

NA Selank Structure

1. Enhanced Enzymatic Stability

The N-terminal acetyl group on NA Selank shields the threonine alpha-amine from aminopeptidase recognition, a primary entry point for rapid degradation of native Selank in plasma and brain tissue preparations. Research models indicate that this modification extends the functional half-life of the peptide in laboratory matrices, supporting experimental designs that require longer-duration exposure than is feasible with the parent sequence.

2. Modified GABAergic-Binding Profile

Native Selank is studied for its influence on GABAergic neurotransmission through subtype-selective, concentration-dependent mechanisms. Acetylation of the N-terminus in NA Selank alters the local electrostatic and steric environment around the threonine and lysine residues, and research models indicate that this can modify the GABAergic-binding profile of the heptapeptide. Comparative experiments examine how the modification reshapes the influence of the peptide on adaptive-signalling and stress-response readouts.

3. Tuftsin-Derived Immune Signaling

The Thr-Lys-Pro-Arg motif at the N-terminal end of Selank carries the tuftsin recognition sequence associated with macrophage and lymphocyte signaling. N-acetylation in NA Selank caps this terminus and modifies its interaction with tuftsin-related immune pathways, including cytokine balance and T-helper cell signaling. Research models examine how these chemical changes influence neuro-immune communication and post-infectious immune regulation in laboratory contexts.

4. Neurotrophic and Gene-Expression Research

Like its parent compound, NA Selank is investigated for its influence on BDNF expression and gene-expression profiles in central nervous system tissue. Comparative transcriptomic experiments examine how N-terminal acetylation reshapes the patterns of gene regulation previously reported for native Selank, including genes related to GABAergic neurotransmission, inflammatory signaling, and neurotrophic factor pathways.

Research Applications

Conclusion

NA Selank is a chemically stabilized analog of Selank in which N-terminal acetylation extends proteolytic resistance and reshapes interactions across GABAergic, tuftsin-related immune, and neurotrophic signaling pathways. Through its modified stability profile and altered binding chemistry, NA Selank serves as a research tool for investigating how N-terminal chemistry contributes to tuftsin-derived heptapeptide function and for comparative studies alongside the parent molecule.

Research Use Disclaimer

This product is intended for research and laboratory use only. It is designed exclusively for in vitro research purposes. All information provided is for educational and research reference only. This product is not intended for human or animal use. It is not a drug, food, or cosmetic and must not be marketed, labeled, or used as such. Use and handling are restricted to trained and qualified professionals.