Dynorphin A (1-17)

Also known as Dyn A (1–17); Dynorphin A

Full-length, 17-residue dynorphin A, a prodynorphin-derived ligand used to investigate κ-opioid signalling and peptide processing.

Length: 17 amino acids
Half-life: Not well characterised
Mechanism: Dynorphin A (1-17) preferentially activates κ-opioid receptors, engaging Gi/o-dependent inhibition of adenylyl cyclase and modulation of neuronal ion channels. It can also interact with other opioid receptors and produce non-opioid effects under some experimental conditions, so it is not an absolutely selective κ-receptor probe.
Studied in: Recombinant κ-receptor assays, neuronal cultures, spinal cord preparations and rodent models study dynorphin A signalling, proteolysis and opioid-independent cellular effects.

About Dynorphin A (1-17)

Dynorphin A (1-17) is the full-length 17-residue form of dynorphin A, with the sequence Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-Pro-Lys-Leu-Lys-Trp-Asp-Asn-Gln. It is generated by proteolytic processing of prodynorphin, the precursor that also gives rise to dynorphin B and related peptides. The first five residues match leucine-enkephalin, while the basic C-terminal extension contributes importantly to its pharmacology. Dynorphin was originally identified through strong opioid activity in pituitary extracts, followed by sequence characterisation.

Although commonly used as an endogenous κ-opioid receptor ligand, dynorphin A requires careful interpretation in complex preparations. Receptor abundance, peptide degradation and assay conditions can alter the apparent contribution of opioid receptor subtypes. Non-opioid actions involving excitatory signalling and membrane interactions have also been investigated, particularly under conditions that favour such effects. Comparing the intact peptide with shorter fragments, including dynorphin A (1–8), helps separate sequence-dependent receptor activity from broader cellular responses.

Laboratory notes

Confirm that the material is the 1–17 peptide rather than the frequently studied 1–8 or 1–13 fragments.
Assess recovery from assay vessels; this basic peptide may adsorb to surfaces, affecting the free concentration.
Combine κ-receptor antagonism with receptor-null controls and peptide-integrity measurements when investigating non-opioid readouts.

Storage and reconstitution basics: storage guide.

Questions about Dynorphin A (1-17)

What does the designation 1-17 specify?

It identifies residues 1 through 17 of dynorphin A, distinguishing the full-length peptide from shorter N-terminal fragments.

Is dynorphin A exclusively selective for κ-opioid receptors?

No. It preferentially engages κ-opioid receptors, but other opioid receptors and non-opioid mechanisms can contribute in some experimental systems.

Why is the basic C-terminal region important?

Its arginine and lysine residues influence receptor interactions, surface adsorption and membrane associations, making the full peptide distinct from leucine-enkephalin.

Is Dynorphin A (1-17) for human use?

No. It is supplied strictly for in-vitro laboratory research and is not for human or animal consumption.

Related research peptides

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