Neuropeptide Y (29-64), amide, human TFA

Neuropeptide Y (29-64), amide, human (TFA) is involved in Alzheimer's disease (AD) and protects rat cortical neurons against β-Amyloid toxicity.

Designed for biological research and industrial applications, not intended for individual clinical or medical purposes.

CAT No: R1546

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M.F/Formula
C₁₉₁H₂₈₆F₃N₅₅O₅₉S
M.W/Mr.
4385.70
Sequence
One Letter Code: YPSKPDNPGEDAPAEDMARYYSALRHYINLITRQRY-NH2
three Letter Code: Tyr-Pro-Ser-Lys-Pro-Asp-Asn-Pro-Gly-Glu-Asp-Ala-Pro-Ala-Glu-Asp-Met-Ala-Arg-Tyr-Tyr-Ser-Ala-Leu-Arg-His-Tyr-Ile-Asn-Leu-Ile-Thr-Arg-Gln-Arg-Tyr-NH2

Neuropeptide Y (29-64), amide, human TFA is a synthetic peptide fragment corresponding to amino acids 29 through 64 of the human neuropeptide Y (NPY) sequence, amidated at the C-terminus and supplied as a trifluoroacetate (TFA) salt. As a biologically relevant peptide segment, it retains key structural motifs associated with the functional domains of full-length NPY, a highly conserved neuropeptide involved in central and peripheral signaling. The 29-64 fragment has been widely utilized in neurobiological, pharmacological, and receptor-binding studies to dissect the roles of specific peptide regions in receptor interaction, signal transduction, and modulatory activity. Its defined sequence and amidation make it a valuable tool for researchers investigating the structure-function relationships and biological mechanisms of neuropeptide Y family members.

Receptor binding studies: In neuropharmacology, the 29-64 fragment is frequently employed to investigate the binding specificity and affinity of NPY receptors, particularly Y1, Y2, and Y5 subtypes. By isolating the C-terminal region, researchers can assess which peptide domains are critical for high-affinity receptor interaction, facilitating the mapping of ligand-receptor contacts and the development of selective agonists or antagonists. This approach is instrumental in elucidating the molecular determinants of peptide-receptor recognition and downstream signaling pathways.

Structure-activity relationship (SAR) analysis: The truncated peptide serves as a model system for dissecting the structural requirements underlying NPY's biological activity. Using the 29-64, amide fragment, scientists can perform comparative studies with full-length and other truncated peptides to determine the minimal sequence necessary for receptor activation or inhibition. Such SAR investigations yield important insights into the conformational dynamics, secondary structure, and functional motifs responsible for neuropeptide efficacy, informing the rational design of novel peptide analogs.

Peptide-receptor signaling research: The amide-modified C-terminal fragment is used in cellular assays to probe the activation of intracellular signaling cascades following NPY receptor engagement. By applying the peptide in vitro to cultured neurons or transfected cell lines expressing specific receptor subtypes, researchers can monitor downstream effects such as cAMP modulation, calcium flux, or kinase activation. These studies help delineate the mechanistic pathways through which NPY influences neuronal excitability, neurotransmitter release, and other physiological processes.

Peptide synthesis and analytical standards: As a chemically defined peptide segment, the 29-64, amide variant is utilized as a reference standard in peptide synthesis and analytical method development. It provides a benchmark for validating synthetic protocols, optimizing purification strategies, and calibrating analytical instruments such as HPLC and mass spectrometry. The availability of this fragment supports quality control in peptide production and facilitates the characterization of related neuropeptide derivatives.

Functional studies of neuropeptide processing: The 29-64 fragment is also valuable in exploring the enzymatic processing and post-translational modification of neuropeptides. By serving as a substrate or comparative control in enzymatic assays, it aids in identifying the specific proteolytic events and modification patterns that regulate NPY maturation, stability, and bioactivity. These investigations contribute to a deeper understanding of neuropeptide biosynthesis and the regulatory mechanisms governing peptide signaling in neuronal and endocrine contexts.

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