AC-Selank-NH2 (10mg)

Description

AC-Selank-NH2 (10mg) – Research Compound

Disclaimer: This compound is provided strictly for laboratory and scientific research purposes only. It is not approved by the U.S. Food and Drug Administration (FDA) for human or veterinary use, including ingestion, injection, or any form of administration.

Chemical Properties of the Compound

Overview

AC-Selank-NH2 (N-Acetyl Selank Amidate; Ac-TKPRPGP-NH2) is a synthetic heptapeptide. It is a structurally modified analog of Selank, a compound developed by the Institute of Molecular Genetics of the Russian Academy of Sciences. Selank itself is a synthetic analog of the endogenous immunomodulatory tetrapeptide tuftsin (Thr-Lys-Pro-Arg), extended at the C-terminus with a Pro-Gly-Pro sequence to enhance metabolic stability. AC-Selank-NH2 incorporates two additional structural modifications relative to parent Selank: N-terminal acetylation, which confers resistance to aminopeptidase-mediated degradation, and C-terminal amidation, which confers resistance to carboxypeptidase-mediated degradation. These modifications have been investigated in preclinical contexts for their effects on enzymatic half-life and receptor interaction profile. Regulatory agencies, including the U.S. Food and Drug Administration (FDA), have not approved AC-Selank-NH2 for human or veterinary use, including ingestion, injection, or any form of administration. It is not a dietary supplement or consumer product. Availability is restricted to qualified researchers and licensed laboratory institutions. Clinical research initiatives involving this compound require guidance from the relevant Institutional Review Board (IRB), and preclinical animal studies must comply with IACUC directives under the Animal Welfare Act (AWA).

Working Mechanism of AC-Selank-NH2

In preclinical models, Selank and its structural analogs have been investigated for their interactions with GABAergic neurotransmission pathways. In vitro studies in IMR-32 neuroblastoma cell cultures have examined the effects of Selank on the expression of genes involved in GABAergic neurotransmission, with observations indicating that Selank modulates the transcriptional profile of GABAergic system components in a pattern broadly correlated with GABA itself in qPCR-based gene expression analyses. The acetylated and amidated modifications of AC-Selank-NH2 are understood to alter the peptide’s susceptibility to enzymatic degradation, potentially affecting receptor interaction duration relative to unmodified Selank in in vitro degradation assays. [Volkova et al., 2016]

At the neuropeptide signaling level, Selank has been investigated in preclinical behavioral models for enkephalin metabolism interactions, with proposed mechanisms involving inhibition of enkephalin-degrading enzymes, which may indirectly sustain endogenous GABAergic tone. Separately, preclinical rodent studies have examined Selank’s effects on brain-derived neurotrophic factor (BDNF) expression in ethanol withdrawal models, with reported associations between Selank administration and changes in BDNF regulation in hippocampal regions under experimental conditions. [Kolik et al., 2019]

These interactions remain under investigation, with variability across experimental models and no fully established mechanism confirmed in any human clinical context.

Research Findings / Research Applications

Preclinical investigations have examined AC-Selank-NH2 and its parent compound Selank in relation to:

GABAergic Gene Expression Modulation in Neuroblastoma Cell Models:

In vitro studies conducted in IMR-32 neuroblastoma cell cultures examined the effects of Selank on the expression of 84 genes involved in GABAergic neurotransmission using qPCR methodology. Observed changes in gene expression showed a strong positive correlation with GABA-induced transcriptional patterns across the 84-gene panel (with Selank-treated cultures producing expression profiles that broadly paralleled GABA administration at the transcriptional level), suggesting that Selank’s influence on GABAergic signaling may occur at the level of gene expression regulation rather than exclusively through direct receptor binding. These findings have been investigated as a potential basis for the peptide’s observed lack of sedation relative to classical benzodiazepine GABAergic modulators in rodent behavioral models. [Volkova et al., 2016]

BDNF Expression and Ethanol Withdrawal Research in Rodent Models:

Selank has been investigated in rodent models of ethanol-induced cognitive disruption and withdrawal. Preclinical observations reported by Kolik et al. (2019) examined associations between Selank administration and BDNF expression regulation in hippocampal regions under ethanol withdrawal conditions, with findings suggesting a connection between the peptide’s activity and neurotrophic factor modulation in stress-related models. These findings have been examined in the context of neuroplasticity-related neuropeptide pharmacology. [Kolik et al., 2019]

Anxiolytic-Like Activity in Rodent Behavioral Paradigms:

Selank has been examined in standard preclinical rodent behavioral paradigms, including elevated plus-maze and open-field models. Observed anxiolytic-like effects in these models were reported without concurrent motor impairment, sedation, or amnesic effects in treated animals. This is a pharmacological separation not consistently observed with benzodiazepine reference compounds in the same experimental systems. These observations have been investigated in the context of neuropeptide-based anxiolytic pharmacology research. [Volkova et al., 2016]

Immunomodulatory and Cytokine Pathway Investigation:
Given its structural origin as a tuftsin analog, Selank has been examined in preclinical and in vitro settings for its interactions with immunomodulatory pathways. Observations have included examination of its effects on interleukin expression and cytokine profile modulation in rodent and cell culture models, with investigations positioned within the context of neuropeptide-immune system interaction research rather than any clinical immunological application.

Peptide Stability and Enzymatic Resistance Assays:

The structural modifications incorporated into AC-Selank-NH2 (N-terminal acetylation and C-terminal amidation) have been examined as a model for studying terminal protection strategies in peptide chemistry. In vitro stability assays have investigated the compound’s resistance to aminopeptidase and carboxypeptidase activity compared to unmodified peptide analogs, with such research contributing to broader investigations of peptide engineering for improved in vitro and in vivo experimental half-life.

Serotonergic Pathway Investigation in Murine Stress Models:

Selank has been examined in preclinical murine models for its interactions with serotonergic neurotransmitter pathways. In tryptophan depletion models designed to reduce central serotonin availability, Selank administration was observed to modulate serotonin metabolism in brainstem regions implicated in neurotransmitter regulation, with findings positioned within the context of neuropeptide-monoamine interaction research. These observations have been investigated as a potential secondary mechanism contributing to the broader neurochemical profile of Selank-class peptides in preclinical stress models. [Volkova et al., 2016]

Note: These findings are based on early-stage and preclinical research. Results are not consistent across all models, and data remains limited without validation in human clinical settings.

Risks & Handling Information

• Risk Tier: MODERATE-HIGH. AC-Selank-NH2 is a CNS-active neuropeptide investigated for interactions with GABAergic neurotransmission pathways in preclinical models. Its acetylated and amidated structural modifications may confer enhanced enzymatic resistance relative to the parent compound, with potential implications for receptor interaction duration that are not fully characterized. The full toxicological and off-target interaction profile of AC-Selank-NH2 in biological systems has not been established. Any unintentional exposure should be treated as requiring immediate decontamination and medical consultation.
• PPE Requirement: The use of appropriate personal protective equipment (PPE) (including nitrile gloves, lab coat, and eye protection) is essential in conducting all experiments involving this compound.
• Controlled Environment: Handling should occur within controlled laboratory environments designed for research activities, with adequate ventilation and appropriate containment measures in place at all times.
• Exposure Prohibition: Do not inhale, ingest, or make direct skin contact with the compound. This material is not intended for any form of self-administration or non-laboratory exposure under any circumstances.
• Toxicological Status: The toxicological profile of AC-Selank-NH2 is not fully established. Exposure risks remain uncertain due to limited long-term safety data. As a CNS-active peptide with GABAergic pathway interactions observed in preclinical models, researchers should adhere to institutional biosafety protocols applicable to centrally active neuropeptide compounds.
• Storage and Degradation Risk: Improper storage conditions, including exposure to heat, light, or moisture, may result in compound degradation and compromised sample integrity. Maintain lyophilized vials at −20°C until use, and adhere to recommended reconstitution protocols to preserve research-grade integrity.

FAQs

Q: What is the regulatory status of AC-Selank-NH2 in the United States?

AC-Selank-NH2 has not been approved by the U.S. Food and Drug Administration (FDA) for human or veterinary use, including ingestion, injection, or any form of administration. It is not classified as a dietary supplement or consumer product and is available exclusively for qualified laboratory and scientific research purposes at licensed institutions operating under applicable institutional oversight frameworks.

Q: How does AC-Selank-NH2 differ structurally from parent Selank?

Parent Selank (Thr-Lys-Pro-Arg-Pro-Gly-Pro) carries a free N-terminus and a free C-terminal carboxylic acid. AC-Selank-NH2 incorporates N-terminal acetylation (Ac-) and C-terminal amidation (-NH2), two established peptide chemistry modifications that have been investigated for their effects on aminopeptidase and carboxypeptidase resistance, respectively. These terminal modifications are understood to extend the peptide’s in vitro enzymatic stability relative to the unmodified parent sequence.

Q: What receptor systems has AC-Selank-NH2 been investigated for in preclinical research?

Preclinical research on Selank and its structural analogs has primarily investigated interactions with GABAergic neurotransmission pathways, including effects on GABAergic gene expression profiles in neuroblastoma cell models, as well as associations with brain-derived neurotrophic factor (BDNF) regulation and enkephalin metabolism in rodent models. These investigations are conducted in controlled in vitro and preclinical animal settings. [Volkova et al., 2016]

Q: Has AC-Selank-NH2 specifically been evaluated in human clinical trials?

No peer-reviewed human clinical trials specific to the AC-Selank-NH2 modification have been published as of June 2026. Available peer-reviewed research is derived from in vitro cell culture studies and preclinical rodent models using parent Selank or structurally related analogs. Findings from these models have not been validated in human clinical settings, and data remains limited in scope and consistency across experimental systems.

Q: What storage conditions are required to maintain AC-Selank-NH2 integrity for research use?

Lyophilized AC-Selank-NH2 should be stored at −20°C, protected from light and moisture. Following reconstitution in an appropriate aqueous buffer, storage at 2–8°C is recommended with use within 30 days. Repeated freeze-thaw cycles and exposure to elevated temperatures or humidity may result in peptide degradation, compromising experimental data integrity.

Q: Why is a separate CAS number not listed for AC-Selank-NH2?

A dedicated CAS registry number specific to the N-acetylated, C-amidated form of Selank has not been independently assigned in publicly available chemical databases as of June 2026. The compound is identified by its UNII designation (J3PM702O93) and is structurally characterized by its molecular formula (C₃₅H₅₉N₁₁O₁₀) and sequence (Ac-TKPRPGP-NH2). The parent Selank CAS (129954-34-3) and PubChem CID (11765600) are provided for structural reference context.

References

Volkova, A., Shadrina, M., Kolomin, T., Andreeva, L., Limborska, S., Myasoedov, N., & Slominsky, P. (2016). Selank Peptide Administration Affects the Expression of Some Genes Involved in GABAergic Neurotransmission. Frontiers in Pharmacology, 7, 31. https://pubmed.ncbi.nlm.nih.gov/26924987/

Kolik, L. G., Nadorova, A. V., & Seredenin, S. B. (2019). Peptide Selank Prevents Memory and Attention Impairments Caused by Ethanol in Rats: The Role of BDNF. Bulletin of Experimental Biology and Medicine, 167(5), 611–614. https://pubmed.ncbi.nlm.nih.gov/31625062/

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