Evidence map›Paper›PMID 39283368›Full record

ArticleAnalytical and bioanalytical chemistry2024

Towards a universal method for middle-down analysis of antibodies via proton transfer charge reduction-Orbitrap mass spectrometry.

Ryan N Oates, Linda B Lieu, Jake T Kline, Christopher Mullen, Kristina Srzentić, Romain Huguet, Graeme C McAlister, Jingjing Huang, David Bergen, Rafael D Melani and 4 more

Abstract read
In one paragraph

Article in Analytical and bioanalytical chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

9 citing papers in PubMed.

  1. Extending Serum IgG1 Antibody Repertoire Coverage Using DIA-PTCR.Journal of the American Society for Mass Spectrometry · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Top-Down and Middle-Down Mass Spectrometry of Antibodies.Molecular & cellular proteomics : MCP · 2025
    Review
  8. Article
  9. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

14 authors.

Ryan N OatesDepartment Chemistry and Biochemistry, University of Oklahoma, Norman, OK, 73109, USA.
Linda B LieuDepartment Chemistry and Biochemistry, University of Oklahoma, Norman, OK, 73109, USA.
Jake T KlineSchool of Biological Sciences, University of Oklahoma, Richards Hall 411B, 730 Van Vleet Oval, Norman, OK, 73109, USA.
Christopher MullenThermo Fisher Scientific, San Jose, CA, 35134, USA.
Kristina SrzentićThermo Fisher Scientific, CH-4153, Reinach, Switzerland.
Romain HuguetThermo Fisher Scientific, San Jose, CA, 35134, USA.
Graeme C McAlisterThermo Fisher Scientific, San Jose, CA, 35134, USA.
Jingjing HuangThermo Fisher Scientific, San Jose, CA, 35134, USA.
David BergenThermo Fisher Scientific, San Jose, CA, 35134, USA.
Rafael D MelaniThermo Fisher Scientific, San Jose, CA, 35134, USA.
Vlad ZabrouskovThermo Fisher Scientific, San Jose, CA, 35134, USA.
Kenneth R DurbinProteinaceous, Inc, Evanston, IL, 60626, USA.
John E P SykaThermo Fisher Scientific, San Jose, CA, 35134, USA.
Luca FornelliDepartment Chemistry and Biochemistry, University of Oklahoma, Norman, OK, 73109, USA. luca.fornelli@ou.edu.ORCID http://orcid.org/0000-0001-6334-1046

Funding

A multi-level mass spectrometry pipeline for the analysis of whole proteoforms and their complexesR35GM147397 · NIGMS · UNIVERSITY OF OKLAHOMA · PI Luca Fornelli · 2022 to 2026
$1.9M
NIGMS NIH HHS R35 GM147397NIGMS NIH HHS R35GM147397
6 · The paper itself

Abstract

Modern mass spectrometry technology allows for extensive sequencing of the ~ 25 kDa subunits of monoclonal antibodies (mAbs) produced by IdeS proteolysis followed by disulfide bond reduction, an approach known as middle-down mass spectrometry (MD MS). However, the spectral congestion of tandem mass spectra of large polypeptides dramatically complicates fragment ion assignment. Here, we report the development and benchmark of an MD MS strategy based on the combination of different ion fragmentation techniques with proton transfer charge reduction (PTCR) to simplify the gas-phase sequencing of mAb subunits. Applied on the liquid chromatography time scale using an Orbitrap Tribrid mass spectrometer, PTCR produces easy-to-interpret mass spectra with limited ion signal overlap. We demonstrate that the accurate estimation of the number of charges submitted to the Orbitrap mass analyzer after PTCR allows for the detection of charge-reduced product ions over a wide mass-over-charge (m/z) window with low parts per million m/z accuracy. Therefore, PTCR-based MD MS analysis increases not only sequence coverage, number of uniquely identified fragments, and number of assigned complementary ion pairs, but also the general confidence in the assignment of subunit fragments. This data acquisition method can be readily applied to any class of mAbs without an apparent need for optimization, and benefits from the high resolving power of the Orbitrap mass analyzer to return sequence coverage of individual subunits exceeding 80% in a single run, and > 90% when just two experiments are combined.

Indexed as

Antibodies, MonoclonalProtonsAmino Acid SequenceChromatography, LiquidMass SpectrometryTandem Mass SpectrometryAntibodies, MonoclonalProtonsETDEThcDFourier transform mass spectrometry, FTMSHCDIgGMiddle-downMonoclonal antibody, mAbOrbitrapOrbitrap EclipseProton transfer charge reduction, PTCR

Identifiers

PMID39283368
PMCPMC11837950

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Registered trials

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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.