Opioid drugs, such as morphine and heroin, are widely used; both medicinally as analgesics, and illicitly as narcotics. Despite the extensive use of these drugs, relatively little is understood about how they activate their target protein – the μ-opioid receptor.

This study between the labs of Prof Eamonn Kelly (School of Physiology, Pharmacology & Neuroscience) and Dr Richard Sessions (School of Biochemistry), addresses the molecular actions of a clinically important opioid, buprenorphine, and its analogues.

Using a combination of modelling of the μ-opioid receptor, and in vitro cellular signalling assays, this study shows that although the drugs share a similar chemical structure, they bind to the receptor in distinct positions, and this may affect the signalling outcome.

This study builds on a body of literature which aims to untangle the complex signalling of the μ-opioid receptor. A greater understanding of the molecular mechanism by which opioids activate their receptor will aid the development of new opioid analgesics, with greater therapeutic benefit and reduced side effects.

Katy Sutcliffe, SWBio DTP student

Paper: Drug binding poses relate structure with efficacy in the mu opioid receptor by K.J. Sutcliffe, G. Henderson, E. Kelly and R.B. Sessions, in the Journal of Molecular Biology.