Biotin-Dynorphin A (1-17) Peptide Fragment

Product Name: Biotin-Dynorphin A (1-17) Peptide Fragment

Sequence One Letter Code: Biotin-YGGFLRRIRPKLKWDNQ

Sequence Three Letter Code: Biotin-Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-Pro-Lys-Leu-Lys-Trp-Asp-Asn-Gln-OH

Chemical Formula:C109H169N33O25S

Molecular Weight: 2373.9

Purity: 95%

Form: Lyophilized

Storage Conditions: - 20 °C

Research Area: Neurological Disease Research

Source / Species: pig

Conjugation: Conjugated

Conjugation Type: Biotins

Code Nacres: NA.26

Application: Biotin–Dynorphin A (1–17) is a biotinylated opioid peptide fragment derived from prodynorphin and generated through proprotein convertase processing. This peptide primarily activates the κ-opioid receptor, mediating effects on pain perception, stress response, and reward pathways. Biotin conjugation facilitates affinity capture, receptor binding analysis, and pull-down assays using streptavidin-based systems. It is widely applied in neuroscience and pharmacology research to examine KOR signaling mechanisms and opioid peptide interactions.

Current Research: Biotin–Dynorphin A (1–17) is a biotin-conjugated form of the endogenous opioid peptide fragment Dynorphin A (1–17), generated from the prodynorphin precursor through proprotein convertase processing. This 17–amino acid fragment retains the full N-terminal opioid pharmacophore and exhibits potent agonist activity at the κ-opioid receptor (KOR), a Gi/o-coupled G protein–coupled receptor widely expressed in the central and peripheral nervous systems. Biotinylation enables high-affinity interaction with streptavidin-based platforms, facilitating biochemical detection, affinity purification, and receptor-binding analyses without substantially altering the peptide’s functional core. Biological Context Dynorphin A peptides are key endogenous ligands within the opioid system and are particularly associated with κ-opioid receptor signaling. Activation of KOR by Dynorphin A (1–17) results in: Inhibition of adenylyl cyclase and reduced intracellular cAMP Activation of GIRK channels leading to neuronal hyperpolarization Inhibition of voltage-gated calcium channels Modulation of ERK and p38 MAPK pathways These signaling events influence nociception, stress adaptation, affective states, and reward processing. Functional Advantages of Biotin Conjugation The addition of biotin provides several analytical and biochemical advantages: Affinity capture using streptavidin-coated beads or plates Stable immobilization for receptor-binding assays Compatibility with ELISA-style detection systems Pull-down of receptor complexes or interacting proteins Because the biotin–streptavidin interaction is exceptionally strong (Kd ~10⁻¹⁵ M), Biotin–Dynorphin A (1–17) is particularly suitable for robust affinity-based workflows. Research Applications 1. Receptor Binding and Pharmacological Studies Biotin–Dynorphin A (1–17) can be immobilized or detected via streptavidin-linked reporters to assess KOR binding affinity, receptor occupancy, and competitive displacement by antagonists or biased agonists. 2. Pull-Down and Protein Interaction Assays The peptide supports identification of receptor-associated complexes or interacting proteins in cell lysates, aiding characterization of KOR-associated signaling assemblies. 3. Receptor Internalization and Trafficking Studies When combined with fluorescent streptavidin probes, the biotinylated peptide enables visualization of ligand-induced receptor internalization and trafficking dynamics in cell-based systems. 4. Signal Transduction Analysis Biotin–Dynorphin A (1–17) can be used to stimulate KOR-expressing cells while allowing parallel biochemical detection, supporting integrated analysis of ligand engagement and downstream signaling events. Experimental Considerations The site of biotin conjugation may influence receptor-binding kinetics; validation against the non-biotinylated peptide is recommended in quantitative pharmacological studies. Proper controls, including excess free ligand competition, can confirm binding specificity. Peptide handling should minimize proteolytic degradation to preserve activity.