Dynorphins

Dynorphins are a class of opioid peptides that arise from the precursor protein prodynorphin. When prodynorphin is cleaved during processing by proprotein convertase, multiple active peptides are released: dynorphin A, dynorphin B, and α/β-neoendorphin.

Function[edit | edit source]

Dynorphins are involved in modulating responses to pain, regulating emotion, and maintaining homeostasis. They are endogenous ligands for the kappa opioid receptor, which is one of the four related receptors that bind opioid-like compounds in the brain and are responsible for mediating the effects of these compounds. These include analgesia, diuresis, and sedation.

Structure[edit | edit source]

Dynorphin A and B are both peptides that are made up of amino acids. Dynorphin A is a 17-amino acid peptide, while dynorphin B, also known as rimorphin, is a 13-amino acid peptide. Both peptides share the same N-terminal sequence, which is thought to be responsible for their opioid activity.

Clinical significance[edit | edit source]

Dynorphins have been implicated in a number of clinical conditions. They have been found to play a role in mood disorders, addiction, and neurodegenerative diseases. In particular, alterations in dynorphin function or the kappa opioid receptor have been linked to depression, anxiety, and schizophrenia.

Research[edit | edit source]

Research into dynorphins and the kappa opioid receptor is ongoing, with the aim of developing new treatments for conditions such as depression and addiction. Some studies have suggested that targeting the kappa opioid receptor could be a potential strategy for treating these conditions.

References[edit | edit source]

Dynorphins Resources
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