Premium
Rapid fingerprinting of a highly glycosylated fusion protein by microfluidic chip‐based capillary electrophoresis–mass spectrometry
Author(s) -
Deyanova Ekaterina G.,
Huang Richard Y.C.,
Madia Priyanka A.,
Nandi Pradyot,
Gudmundsson Olafur,
Chen Guodong
Publication year - 2021
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.202000132
Subject(s) - glycosylation , chemistry , mass spectrometry , chromatography , capillary electrophoresis , microfluidics , fusion protein , n linked glycosylation , biochemistry , glycoprotein , recombinant dna , nanotechnology , materials science , glycan , gene
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.