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Articles by Eric Largy
A protein–foldamer supramolecular synthon for self-assembled hybrid architectures
Abstract Constructing artificial assemblies that combine proteins and synthetic ligands has been hampered by the lack of protein–ligand interfaces that are sufficiently large and organized to enable precise structural control. Here ribosome display selection is used to identify a protein that binds a helical aromatic foldamer both tightly and selectively through a sizeable surface area. We used this complex as a supramolecular synthon to create well-defined hybrid foldamer–protein architectures.
A General Framework to Interpret Hydrogen-Deuterium Exchange Native Mass Spectrometry of G-Quadruplex DNA
Download Hi-Res ImageDownload to MS-PowerPointCite This:J. Am. Chem. Soc. 2023, XXXX, XXX Terms & Conditions Most electronic Supporting Information files are available without a subscription to ACS Web Editions. Such files may be downloaded by article for research use (if there is a public use license linked to the relevant article, that license may permit other uses).
A General Framework to Interpret Hydrogen-Deuterium Exchange Native Mass Spectrometry of G-Quadruplex DNA
Abstract G-quadruplexes (G4s) are secondary structures formed by guanine-rich oligonucleotides involved in various biological processes. However, characterizing G4s is challenging because of their structural polymorphism. Here, we establish how hydrogen-deuterium exchange native mass spectrometry (HDX/MS) can help to characterize G4 structures and dynamics in solution. We correlated the time range of G4 exchange to the number of guanines involved in inner and outer tetrads.
Native Hydrogen/Deuterium Exchange Mass Spectrometry of Structured DNA Oligonucleotides
Download Hi-Res ImageDownload to MS-PowerPointCite This:Anal. Chem. 2020, XXXX, XXX RETURN TO ARTICLES ASAPPREVArticleNEXT Eric Largy* Eric Largy University of Bordeaux, INSERM and CNRS, Laboratoires Acides Nucléiques: Régulations Naturelle et Artificielle (ARNA, U1212, UMR5320), IECB, 2 rue Robert Escarpit, 33600 Pessac, France *Email: .
Epitope Mapping of an Interleukin Receptor for Three Therapeutic Antibodies by Hydrogen-Deuterium Exchange Mass Spectrometry
The study of protein-protein interactions is critical in the development of biotherapeutics, to develop new candidates, to understand modes of actions, and to protect intellectual property. Among all the analytical techniques available for epitope mapping studies, hydrogen–deuterium exchange mass spectrometry (HDX-MS) is usually faster and easier to carry out.
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