Membrane proteins are difficult to study outside the lipid bilayer, where conventional detergents can disrupt their structure, interactions, and associated lipids. Our laboratory developed peptide-based membrane mimetics that provide alternative ways to extract and stabilize membrane proteins. Peptidiscs surround the membrane-exposed surface of proteins after extraction, creating stable, water-soluble particles that adapt to proteins of different sizes and shapes. More recently, Peptergents have extended this approach by enabling membrane proteins to be extracted directly from biological membranes without conventional detergents. Together, these technologies provide a foundation for studying membrane proteins from individual purified complexes to entire membrane proteomes.
KEY PUBLICATIONS
The Peptidisc, a simple method for stabilizing membrane proteins in detergent-free solution. Carlson ML, Young JW, Zhao Z, Fabre L, Jun D, Li J, Li J, Dhupar HS, Wason I, Mills AT, Beatty JT, Klassen JS, Rouiller I, Duong F. eLife. 2018;7:e34085. doi:10.7554/eLife.34085.
New approach for membrane protein reconstitution into peptidiscs and basis for their adaptability to different proteins. Angiulli G, Dhupar HS, Suzuki H, Wason IS, Duong Van Hoa F, Walz T. eLife. 2020;9:e53530. doi:10.7554/eLife.53530.
PEPTERGENT: A Peptide-Based Reagent for Detergent-Free Extraction of Membrane Proteins and Purification of Membrane Proteomes. Antony F, Bhattacharya A, Duong van Hoa F. Bio-protocol. 2026;16(10):e5700. doi:10.21769/BioProtoc.5700.
A detergent-free workflow for native membrane proteomics using Peptergents. Antony F, Bhattacharya A, Aoki H, Babu M, Duong van Hoa F. bioRxiv. 2026.08.12.744532. doi:10.64898/2026.08.12.744532. Preprint.