Rapid fingerprinting of a highly glycosylated fusion protein by microfluidic chip‐based capillary electrophoresis–mass spectrometry

Protein glycosylation can impact the efficacy, safety, and pharmacokinetics of therapeutic proteins. Achieving uniform and consistent protein glycosylation is an important requirement for product quality control at all stages of therapeutic protein drug discovery and development. The development of...

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Veröffentlicht in:Electrophoresis 2021-02, Vol.42 (4), p.460-464
Hauptverfasser: Deyanova, Ekaterina G., Huang, Richard Y.‐C., Madia, Priyanka A., Nandi, Pradyot, Gudmundsson, Olafur, Chen, Guodong
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container_end_page 464
container_issue 4
container_start_page 460
container_title Electrophoresis
container_volume 42
creator Deyanova, Ekaterina G.
Huang, Richard Y.‐C.
Madia, Priyanka A.
Nandi, Pradyot
Gudmundsson, Olafur
Chen, Guodong
description Protein glycosylation can impact the efficacy, safety, and pharmacokinetics of therapeutic proteins. Achieving uniform and consistent protein glycosylation is an important requirement for product quality control at all stages of therapeutic protein drug discovery and development. The development of a new microfluidic CE device compatible with MS offers a fast and sensitive orthogonal mode of high‐resolution separation with MS characterization. Here, we describe a fast and robust chip‐based CE‐MS method for intact glycosylation fingerprinting of a therapeutic fusion protein with complex sialylated N and O‐linked glycoforms. The method effectively separates multiple sialylated glycoforms and offers a rapid detection of changes in glycosylation profile in 6 min.
doi_str_mv 10.1002/elps.202000132
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subjects CE‐MS
Electrophoresis
Fingerprinting
Glycoprofiling
Mass spectrometry
Microfluidics
Proteins
Quality control
Therapeutic proteins
title Rapid fingerprinting of a highly glycosylated fusion protein by microfluidic chip‐based capillary electrophoresis–mass spectrometry
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