N-Acetyl-Selank is a synthetic analog of a human tetrapeptide tuftsin and classified as a nootropic, anxiolytic peptide. It may be used as a treatment for generalized anxiety disorder.
CAT No: 10-101-258
Synonyms/Alias:N-ACETYL SELANK; J3PM702O93; (AC-THR-LYS-PRO-ARG-GLY-PRO); (2S)-1-(2-(((2S)-1-((2S)-2-(((2S)-1-((2S)-2-(((2S,3R)-2-ACETAMIDO-3-HYDROXY-BUTANOYL)AMINO)-6-AMINO-HEXANOYL)PYRROLIDINE-2-CARBONYL)AMINO)-5-GUANIDINO-PENTANOYL)PYRROLIDINE-2-CARBONYL)AMINO)ACETYL)PYRROLIDINE-2-CARBOXYLIC ACID
N-acetyl Selank is a synthetic peptide derivative belonging to the class of heptapeptide analogs, structurally related to the endogenous tetrapeptide tuftsin. Its acetylated form enhances metabolic stability, making it particularly valuable for biochemical studies involving neuropeptide function and peptide-receptor interactions. As a research-use-only compound, N-acetyl Selank is recognized for its unique sequence and structural properties, which have enabled detailed investigations into peptide signaling pathways, neurochemical modulation, and receptor binding specificity. The compound's resilience against enzymatic degradation and its affinity for certain central nervous system targets have positioned it as a key tool in the exploration of peptide-based regulatory mechanisms in neurobiology and molecular pharmacology.
Neuropeptide signaling research: N-acetyl Selank is frequently employed in studies dissecting the molecular mechanisms underlying neuropeptide-mediated communication within the central nervous system. Its structural similarity to tuftsin permits researchers to probe the modulation of neurotransmitter systems, such as those involving GABAergic and serotonergic pathways. By serving as a stable model peptide, it enables the elucidation of receptor-ligand interactions, downstream signaling cascades, and the role of peptide analogs in synaptic plasticity and neural network regulation.
Peptide structure-activity relationship (SAR) studies: The acetylated modification of Selank provides a valuable scaffold for examining how N-terminal acetylation influences peptide function, receptor affinity, and metabolic stability. Researchers utilize this analog to compare the bioactivity and degradation profiles of native versus modified peptides, thereby gaining insights into the design of more robust neuroactive compounds. Such SAR studies are critical for advancing the understanding of peptide engineering principles and for guiding the rational development of novel research tools.
Enzymatic degradation assays: Due to its enhanced resistance to proteolytic enzymes, N-acetyl Selank serves as a reference standard in experiments assessing peptide stability in biological matrices. Researchers leverage its stability to validate analytical methods, investigate the kinetics of peptide breakdown, and benchmark the effectiveness of enzyme inhibitors. This application is particularly relevant for developing protocols that require prolonged peptide activity or for comparing the metabolic fate of various peptide analogs in vitro.
Receptor binding and affinity profiling: The compound's well-defined sequence and acetylation status make it suitable for in vitro receptor binding assays aimed at quantifying affinity and specificity toward target proteins or receptors. By employing radioligand displacement, fluorescence polarization, or surface plasmon resonance techniques, investigators can characterize the binding kinetics and selectivity of N-acetyl Selank, thereby contributing to the mapping of neuropeptide-receptor interaction landscapes and the identification of novel binding partners.
Peptide-based assay development: The physicochemical properties of N-acetyl Selank, including its solubility and stability, facilitate its use in the optimization of peptide detection and quantification assays. It is commonly incorporated as a calibrant or positive control in mass spectrometry, HPLC, or immunoassay platforms, ensuring reliable performance and reproducibility in analytical workflows. Through such applications, the compound supports the advancement of robust methodologies for peptide analysis in complex biological samples.
1. Urinary Metabolites Associated with Blood Pressure on a Low-or High-Sodium Die
2. High fat diet and GLP-1 drugs induce pancreatic injury in mice
3. Cell-based adhesion assays for isolation of snake venom’s integrin antagonists
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