5th International Conference on Hydrogen Deuterium Exchange Mass Spectrometry (HDXMS2026)

I attended the 5th International Conference on Hydrogen Deuterium Exchange Mass Spectrometry (HDXMS2026), held in Strasbourg, France, from 9 to 13 March 2026. The meeting was organized by the International Society of HDX-MS and covered a broad range of themes, including fundamentals, instrumentation and workflow, biological and biopharmaceutical applications, integrative structural biology, data analysis and statistics, molecular dynamics, and harmonisation/standardisation. The program was built around plenary lectures, short talks, poster sessions, and dedicated workshops with no parallel sessions giving attendees the opportunity to enjoy the full range of scientific topics offered by the organizers.

The scientific level of the conference was particularly high. The invited speaker list alone illustrates the maturity and interdisciplinarity of the field, with contributions from leading scientists. This made the conference especially valuable for obtaining a global view of where HDX-MS currently stands. No longer only as a niche structural biology method, but increasingly as a central analytical tool for probing protein dynamics, interactions, and conformational landscapes in complex biological systems.

Multiple attendees described the field as moving rapidly toward automated data analysis, single-residue or near-residue-level resolution, ultra-sensitive HDX-MS, and more routine integration with molecular dynamics, docking, and other computational approaches. Miklos Guttman explicitly highlighted the latest development and growing interest around scramble-free fragmentation for single-residue HDX-MS, the increasing availability of DIA-based peptide-level analysis tools, the importance of back-exchange effects inside the mass spectrometer, and the broader usefulness of combining HDX-MS with modeling and docking. Mahjoobeh Ehsani reported presenting work on “Quench-enrichment HDX-MS Enables Cellular Protein Structural Dynamics Profiling,” emphasizing the novelty of selective enrichment strategies for in-cell HDX-MS. Daniel Deredge described work integrating machine learning with HDX-MS to model protein-ligand interactions with high accuracy. In parallel, the ProMET project reported active participation in the Standards and Reference Materials workshop, stressing the importance of metrology for the future robustness of HDX-MS measurements. These examples were particularly convincing because they show that HDX-MS is now advancing on several fronts at once: cellular applications, ligand-binding analysis, translational biopharmaceutical use cases, and metrological standardization.

From a personal perspective, this conference was extremely formative in terms of scientific culture and open-mindedness. I was also particularly interested in the epitope mapping dimension and, more broadly, in the way HDX-MS can be used to characterize interaction interfaces and conformational effects in biologically and pharmaceutically relevant systems. Even when not presented strictly under the label of “epitope mapping”, many of the applications discussed at the conference pointed toward the same structural logic: identifying protected regions, describing ligand- or binder-induced conformational changes, and refining mechanistic interpretation at the protein interface level. Although HDX-MS was not initially my main area of expertise, the meeting clearly showed how many bridges can be built with proteomics. There are obvious connections at the level of LC-MS methodology, peptide-centric readouts, data processing, quantitative interpretation, and the broader objective of extracting biologically meaningful information from complex protein systems. For that reason, I found the conference highly enriching beyond the strict boundaries of HDX-MS itself. It broadened my scientific perspective and gave me a better understanding of how structural readouts can complement more classical proteomics workflows.

Another major benefit of this conference was the networking opportunity. Indeed, approximatively 200 international specialists in HDX-MS gathered in Strasbourg. Since this is a field I previously knew only to a limited extent, attending HDXMS2026 allowed me to expand my network in a new scientific community and to identify potential contacts and future partners for integrating structural approaches into future research projects.

Overall, HDXMS2026 was highly beneficial for my scientific development. It provided a broad and up-to-date view of a fast-evolving field, highlighted many conceptual and methodological bridges with proteomics, strengthened my interest in applications such as epitope mapping, and opened concrete perspectives for future collaborations around structural mass spectrometry. I am therefore very grateful to the French Proteomics Society for supporting my participation through this grant!