Intact Proteoform Analysis by Capillary Electrophoresis–Mass Spectrometry. Are We There Yet?

N Noah Gould (Barnett Institute of Chemical and Biological Analysis and Department of Chemistry & Chemical Biology Northeastern University Boston MA USA) Q Qianjie Wang (Department of Chemistry Michigan State University East Lansing MI USA) J Jeffrey N. Agar J Jennifer S. Brodbelt D Daoyang Chen (Discovery Biologics Merck Research Laboratory USA) K Kellye A. Cupp‐Sutton (Department of Chemistry and Biochemistry University of Alabama Tuscaloosa AL USA) E Elena Domínguez‐Vega (Center for Proteomics and Metabolomics Leiden University Medical Center Leiden The Netherlands) F Fei Fang M Marianne Fillet (Laboratory for the Analysis of Medicines Center for Interdisciplinary Research on Medicines (CIRM) University of Liege Quartier Hospital Liege Belgium) M Matthew S Fischer (Department of Chemistry University of Wisconsin‐Madison Madison Wisconsin 53706 USA) A Attila Gáspár Y Ying Ge M Marie‐Jia Gou (Laboratory for the Analysis of Medicines Center for Interdisciplinary Research on Medicines (CIRM) University of Liege Quartier Hospital Liege Belgium) M Michal Greguš C Christoph Gstöttner (Center for Proteomics and Metabolomics Leiden University Medical Center Leiden The Netherlands) N Narmin Hamidli (Department of Inorganic and Analytical Chemistry University of Debrecen Debrecen Hungary) A Amanda Helms (Department of Chemistry, The University of Texas at Austin) M Md Amin Hossain K Kyle J. Juetten (Department of Chemistry University of Texas Austin TX USA) N Neil L. Kelleher (Department of Chemistry) T Tobias Kraus (Department of Chemistry Aalen University Aalen Germany) E Eli J. Larson (Department of Chemistry University of Wisconsin‐Madison Madison Wisconsin 53706 USA) J J. Scott Mellors (908 Devices Inc. Boston MA USA) C Cynthia Nagy (Department of Inorganic and Analytical Chemistry University of Debrecen Debrecen Hungary) C Christian Neusüß (Department of Chemistry Aalen University Aalen Germany) E Erin A. Redman (908 Devices Inc. Boston MA USA) J Jasmin Schairer (Department of Chemistry Aalen University Aalen Germany) S Si Wu T Tian Xu (Department of Chemical and Biomolecular Engineering and Institute for NanoBioTechnology, The Johns Hopkins University, 3400 North Charles Street, Baltimore, Maryland 21218, United States) Z Zhitao Zhao G Guijie Zhu (Department of Chemistry Michigan State University East Lansing MI USA) A Alexander R. Ivanov (Barnett Institute of Chemical and Biological Analysis and Department of Chemistry & Chemical Biology Northeastern University Boston MA USA) K Kevin Jooß (Division of Bioanalytical Chemistry Department of Chemistry and Pharmaceutical Sciences Amsterdam Institute of Molecular and Life Sciences Vrije Universiteit Amsterdam Centre for Analytical Sciences Amsterdam (CASA) Amsterdam The Netherlands) L Liangliang Sun (Department of Chemistry, Michigan State University)

Abstract

Abstract Mass spectrometry (MS)‐based top–down proteomics (TDP) has emerged as a powerful tool for characterizing proteoforms to advance both fundamental and translational research. TDP requires high‐efficiency liquid‐phase separation, high‐resolution MS, and tandem MS. Capillary zone electrophoresis (CZE)‐MS has been proposed as a promising analytical technique for protein analysis decades ago because of its unique and valuable features, including high separation efficiency and high detection sensitivity. However, CZE‐MS has not been widely adopted by the proteomics community, mainly due to concerns with its robustness and reproducibility. Here, we hypothesized that CZE‐MS is sufficiently robust and reproducible for broad adoption due to the continued efforts of the community over the last three decades. In this work, for the first time, research teams from around the world validated the robustness, repeatability, and reproducibility of CZE‐MS for TDP in both simple and complex model proteoform mixtures employing a full spectrum of commercially available capillary electrophoresis (CE)‐MS interfaces, instrumentation, and compared CZE‐MS performance with state‐of‐the‐art liquid chromatography (LC)‐MS methods. This study offers the research community an informative resource of ready‐to‐use experimental CE‐MS techniques and a better understanding of the CZE‐MS approach and its potential in TDP, accelerating the broad adoption of CZE‐MS in proteoform research.

Article Details

Volume / Issue Vol. 65, Issue 5
Published January 28, 2026
ISSN 1433-7851
Publisher Wiley

Journal Info

Angewandte Chemie International Edition

Wiley

ISSN: 1433-7851 Physical Sciences

Authors (34)

N

Noah Gould

Barnett Institute of Chemical and Biological Analysis and Department of Chemistry & Chemical Biology Northeastern University Boston MA USA

Q

Qianjie Wang

Department of Chemistry Michigan State University East Lansing MI USA

J

Jeffrey N. Agar

J

Jennifer S. Brodbelt

D

Daoyang Chen

Discovery Biologics Merck Research Laboratory USA

K

Kellye A. Cupp‐Sutton

Department of Chemistry and Biochemistry University of Alabama Tuscaloosa AL USA

E

Elena Domínguez‐Vega

Center for Proteomics and Metabolomics Leiden University Medical Center Leiden The Netherlands

F

Fei Fang

M

Marianne Fillet

Laboratory for the Analysis of Medicines Center for Interdisciplinary Research on Medicines (CIRM) University of Liege Quartier Hospital Liege Belgium

M

Matthew S Fischer

Department of Chemistry University of Wisconsin‐Madison Madison Wisconsin 53706 USA

A

Attila Gáspár

Y

Ying Ge

M

Marie‐Jia Gou

Laboratory for the Analysis of Medicines Center for Interdisciplinary Research on Medicines (CIRM) University of Liege Quartier Hospital Liege Belgium

M

Michal Greguš

C

Christoph Gstöttner

Center for Proteomics and Metabolomics Leiden University Medical Center Leiden The Netherlands

N

Narmin Hamidli

Department of Inorganic and Analytical Chemistry University of Debrecen Debrecen Hungary

A

Amanda Helms

Department of Chemistry, The University of Texas at Austin

M

Md Amin Hossain

K

Kyle J. Juetten

Department of Chemistry University of Texas Austin TX USA

N

Neil L. Kelleher

Department of Chemistry

T

Tobias Kraus

Department of Chemistry Aalen University Aalen Germany

E

Eli J. Larson

Department of Chemistry University of Wisconsin‐Madison Madison Wisconsin 53706 USA

J

J. Scott Mellors

908 Devices Inc. Boston MA USA

C

Cynthia Nagy

Department of Inorganic and Analytical Chemistry University of Debrecen Debrecen Hungary

C

Christian Neusüß

Department of Chemistry Aalen University Aalen Germany

E

Erin A. Redman

908 Devices Inc. Boston MA USA

J

Jasmin Schairer

Department of Chemistry Aalen University Aalen Germany

S

Si Wu

T

Tian Xu

Department of Chemical and Biomolecular Engineering and Institute for NanoBioTechnology, The Johns Hopkins University, 3400 North Charles Street, Baltimore, Maryland 21218, United States

Z

Zhitao Zhao

G

Guijie Zhu

Department of Chemistry Michigan State University East Lansing MI USA

A

Alexander R. Ivanov

Barnett Institute of Chemical and Biological Analysis and Department of Chemistry & Chemical Biology Northeastern University Boston MA USA

K

Kevin Jooß

Division of Bioanalytical Chemistry Department of Chemistry and Pharmaceutical Sciences Amsterdam Institute of Molecular and Life Sciences Vrije Universiteit Amsterdam Centre for Analytical Sciences Amsterdam (CASA) Amsterdam The Netherlands

L

Liangliang Sun

Department of Chemistry, Michigan State University