Neuropeptide Y (13-36), amide, human

Neuropeptide Y (13-36), amide, human is a synthetic peptide fragment corresponding to residues 13 through 36 of the native human neuropeptide Y, featuring an amidated C-terminus. As a truncated form of the full-length neuropeptide Y, this compound retains a significant portion of the biologically active domain, making it a valuable tool for dissecting receptor subtype selectivity and downstream signaling pathways. Its structural modification and sequence specificity enable researchers to explore the nuanced roles of neuropeptide Y fragments within neurochemical and physiological contexts, particularly in relation to the Y2 and Y5 receptor subtypes. The unique properties of this peptide fragment support its widespread use in neurobiological, pharmacological, and peptide-receptor interaction studies.

Receptor Selectivity Studies: Neuropeptide Y (13-36), amide is widely employed to investigate the selectivity and binding affinity of neuropeptide Y receptor subtypes, especially Y2 and Y5. Unlike the full-length peptide, this fragment preferentially interacts with specific receptors, enabling researchers to delineate the functional contributions and signaling mechanisms of each subtype. Such studies advance understanding of synaptic transmission, neuronal excitability, and the modulation of neurotransmitter release in various regions of the central and peripheral nervous systems.

Peptide-Receptor Interaction Assays: The compound serves as a critical ligand in in vitro and ex vivo binding assays designed to characterize the molecular dynamics between neuropeptide Y fragments and their cognate receptors. Its defined sequence and amidated terminus facilitate reproducible receptor activation or inhibition, making it useful for high-throughput screening of receptor modulators, mapping ligand-binding domains, and elucidating structure-activity relationships. These applications are central to the development of novel pharmacological probes and the refinement of receptor-targeted research tools.

Neurochemical Pathway Analysis: Researchers utilize this peptide fragment to probe the physiological relevance of neuropeptide Y signaling in complex neurochemical networks. By selectively activating or blocking certain receptor subtypes, experiments can reveal the peptide's influence on neurotransmitter systems, such as those involving GABA, glutamate, or catecholamines. Such analyses are instrumental in deciphering the regulatory roles of neuropeptide Y in stress response, appetite control, circadian rhythm, and other central nervous system functions.

Peptide Functional Studies: The defined structure of the (13-36) amide fragment allows for targeted investigations into the biological activity of neuropeptide Y derivatives. Functional assays may include assessments of peptide stability, receptor-mediated intracellular signaling cascades, or the modulation of ion channel activity. These studies provide insight into how specific sequence modifications impact peptide efficacy, receptor activation profiles, and downstream cellular responses, enhancing the rational design of next-generation peptide analogs.

Peptide Synthesis and Analytical Reference: In peptide chemistry and analytical laboratories, neuropeptide Y (13-36), amide, human serves as a reference standard for validating synthetic protocols, purification strategies, and analytical methods such as mass spectrometry or high-performance liquid chromatography. Its well-characterized structure and defined physicochemical properties make it an ideal benchmark for method development, quality control, and comparative studies involving neuropeptide Y analogs or related bioactive peptides.

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