Salipro successfully extracts PANX1 membrane protein

Salipro Biotech, in collaboration with AstraZeneca, has published data from a study which describes a novel method to directly extract membrane proteins from cells into lipid Salipro nanoparticles, enabling structure-function analysis using surface plasmon resonance (SPR) and cryo-electron microscopy (cryo-EM) for challenging drug targets.

The scientists extracted and purified functional membrane proteins directly from cells using the membrane protein PANX1 as a case study. PANX1 is associated with various pathologies, including inflammation, pain, ischaemia, and epilepsy. Exploration of PANX1 as a potential therapeutic target for novel therapeutics has, however, been limited due to overall lack of biophysical studies using isolated systems.   

Stefan Geschwindner, Director of Biophysics, AstraZeneca, said: “Analysing membrane proteins using SPR can pose a challenge due to the inherent instability of these drug targets and the difficulty in immobilising enough functional membrane protein on the biosensor surface to ensure a measurable binding signal. By employing this innovative technique, we were able to confirm target engagement and measure the binding affinities of various pharmacological agents that are known to inhibit PANX1 activity.”  

Robin Löving, CSO of Salipro Biotech, said: “These results provide the basis for further investigations of novel PANX1 binders, leading to the development of more potent and specific compounds to further probe the biology of PANX1 and its potential as a therapeutic target. The novel methodology presented here accelerates the purification of membrane proteins that are ready to generate high-resolution cryo-EM structures, without the need for laborious and time-consuming detergent screenings, protein engineering or inefficient screening of alternative scaffolding set-ups.”

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