Scientific ReportsBiochemistryPeer-reviewed journal article
Discovery of Membrane Channel Modulators via DNA-Encoded Library Screening Using Native-Like Membrane Protein Nanoparticles
Francesco V. ReddavideiD, Trine Lisberg Toft‐BertelseniD, Ieva DrulyteiD, Aspen Rene GutgselliD, Dzung Nguyen, Sara Bonetti, Katerina Vafia, Anne-Sophie Tournillon, Stephan Heiden, Daniel Grosser, Katarina IriciD, Veronica Diez, Nanna MacAulayiD, Stefan GeschwindneriD, Michael ThompsoniD, Jens Frauenfeld, Robin LövingiD
Abstract
Developing novel drugs against membrane proteins is a major challenge in drug discovery due to the difficulty of stabilizing these targets for high-throughput screenings. Pannexin 1 (PANX1) is a membrane channel protein involved in various physiological and pathological processes, making it a promising target for drug discovery. However, efforts to develop PANX1-targeting therapeutics have been hindered by the inherent challenges of stabilizing the protein channel and conducting effective pharmacological screening. Here, we report a proof-of-concept workflow that integrates the Salipro lipid nanoparticle platform with DNA-Encoded Library screenings in a detergent-free format. In this case study, the Salipro DirectMX method was used to generate functional PANX1 nanoparticles for drug discovery and characterisation. Using a high-stringency selection strategy and computational approaches, we identified a specific set of candidate compounds with selective PANX1 enrichment. Surface Plasmon Resonance analysis confirmed the identification of hit compounds. Cryo-Electron Microscopy of the Salipro-PANX1-Compound complex provided structural insights into a potential compound binding site. Electrophysiological recordings in PANX1-expressing Xenopus laevis oocytes demonstrated dose-dependent inhibition of PANX1-mediated ion conductance by the compounds. These findings establish a robust workflow for ligand discovery against challenging membrane protein targets and provide novel chemical starting points for the development of PANX1 modulators.
- organism: Xenopus
- assay: proteomics
- research focus: drug response / drug discovery
- approach: deep learning
- approach: experimental assay
- Citations
- 0
- FWCI
- 0.00
- Field percentile
- 37th percentile
Reproducibility ledger
Nobody has reported trying to reproduce this paper yet. Did you replicate an experiment or run the code? Your report saves the next lab a week.
Sign in to file a reproducibility report.
Related papers
- Direct Cell Extraction of Membrane Proteins for Structure-Function Analysis
I. Drulyte, A. R. Gutgsell, … R. Loving·bioRxiv·Jul 5, 2022
- The Cryo-EM Structure of a Pannexin 1 Channel Reveals an Extracellular Gating Mechanism
Kevin R. Michalski, Johanna Liinamaria Syrjänen, … Toshimitsu Kawate·bioRxiv·Dec 30, 2019
- Ligandability at the membrane interface of GPx4 revealed through a reverse micelle fragment screening platform
Courtney L. Labrecque, Brian Fuglestad·JACS AuPeer-reviewed·Jun 26, 2024
- A Constitutively Closed Pannexin1 Channel in Lipid Bilayer Nanodiscs Assembles as a Large-Pore Heptamer
X. Jin, S. A. Leonhardt, … M. Yeager·bioRxiv·Dec 31, 2020
- Identifying Membrane Protein-Lipid Interactions with Lipidomic Lipid Exchange-Mass Spectrometry
G. Zhang, M. T. Odenkirk, … M. T. Marty·bioRxiv·Jun 2, 2023
- An On-Demand Nanodisc Platform for Reconstitution of Functional Membrane Proteins into Model and Living Membranes
Long-Kai Chen, Yun-Shan Wang, … Chun‐Wei Lin·bioRxiv·Aug 19, 2026