Evidence map›Paper›PMID 42050768›Full record

ArticleRapid communications in mass spectrometry : RCM2026

Resolving Isomeric Structures in Natural Complex Carbohydrates: A Comparative Study of SLIM and Cyclic Ion Mobility Platforms.

Rania Benazza, Christopher P Harrilal, Yehia M Ibrahim, Mathieu Fanuel, David Ropartz, Hélène Rogniaux

Abstract readComparative Study
In one paragraph

Article in Rapid communications in mass spectrometry : RCM, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

6 authors.

Rania BenazzaUR BIA, INRAE, Nantes, France.ORCID https://orcid.org/0000-0002-9616-1225
Christopher P HarrilalBiological Sciences Division, Pacific Northwest National Laboratory, Richland, Washington, USA.
Yehia M IbrahimBiological Sciences Division, Pacific Northwest National Laboratory, Richland, Washington, USA.
Mathieu FanuelUR BIA, INRAE, Nantes, France.
David RopartzUR BIA, INRAE, Nantes, France.
Hélène RogniauxUR BIA, INRAE, Nantes, France.

Funding

AMETHYST project of the PEPR DIADEM, with the financial support from France 2030 program project number ANR-22-PEXD-0015
6 · The paper itself

Abstract

rationaleRecent advances in ion mobility mass spectrometry (IMS) have led to the development of high-resolution platforms such as cyclic IMS and SLIM IMS (structures for lossless ion manipulations), both offering enhanced capabilities for resolving complex biomolecular conformations.

methodsIn this study, these two IMS technologies were evaluated for the characterization of complex natural polysaccharides, using homogalacturonan oligosaccharides (HGOS) derived from plant cell wall pectin as a model system. HGOS were generated through enzymatic depolymerization of the parent polymer and analyzed on both platforms. This approach enabled, for the first time, a direct comparison of mass spectra and ion mobility maps for identical species with varying degrees of polymerization (DP) and methylation (DM).

resultsAs expected, single-pass analyses on the 10-m SLIM IMS provided higher resolving power, allowing a greater number of IMS features to be separated for a given species (e.g., DP5DM4) compared to single-pass cyclic IMS experiments. However, IMS features unresolved in cyclic IMS single-pass mode could be accessed through multi-pass separations. A key distinction between the platforms lies in ion formation and charge state distributions. The SLIM IMS, retrofitted to an Agilent 6560, utilizes a commercial ion source and ion optics that result in the formation of larger and higher charged species, with more cation adducts. While beneficial for resolution, this distribution can dilute signal intensity across multiple charge states, impacting sensitivity. In contrast, the cyclic IMS employs a Z-spray source that favors lower charge states, facilitating more straightforward diagnostic interpretation and characterization. Despite the superior intrinsic IMS resolution of the 10-m SLIM, the combination of ionization behavior, instrument tuning requirements, and data processing complexity makes the cyclic IMS more practical for routine analysis.

conclusionsBoth IMS platforms demonstrated strong capabilities for resolving HGOS structures, highlighting their complementarity and effectiveness in studying complex polysaccharide mixtures.

Indexed as

Ion Mobility SpectrometryOligosaccharidesPectinsIsomerismOligosaccharidesPectinspolygalacturonic acidcarbohydratecyclicIMSoligogalacturonanSLIM

Identifiers

PMID42050768
PMCPMC13125388

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.