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Cited by 334

The DOI matches its Crossref record; 43 of the 43 references it cites were found in a registry or an index.

High-Throughput Profiling of Protein N-Glycosylation by MALDI-TOF-MS Employing Linkage-Specific Sialic Acid Esterification

Reiding, Karli R., Blank, Dennis, Kuijper, Dennis M., Deelder, André M., Wuhrer, Manfred·2014·Analytical Chemistry
DOI 10.1021/ac500335t
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Abstract

Protein glycosylation is an important post-translational modification associated, among others, with diseases and the efficacy of biopharmaceuticals. Matrix-assisted laser desorption/ionization (MALDI) time-of-fight (TOF) mass spectrometry (MS) can be performed to study glycosylation in a high-throughput manner, but is hampered by the instability and ionization bias experienced by sialylated glycan species. Stabilization and neutralization of these sialic acids can be achieved by permethylation or by specific carboxyl group derivatization with the possibility of discrimination between α2,3- and α2,6-linked sialic acids. However, these methods typically require relatively pure glycan samples, show sensitivity to side reactions, and need harsh conditions or long reaction times. We established a rapid, robust and linkage-specific high-throughput method for sialic acid stabilization and MALDI-TOF-MS analysis, to allow direct modification of impure glycan-containing mixtures such as PNGase F-released human plasma N-glycome. Using a combination of carboxylic acid activators in ethanol achieved near-complete ethyl esterification of α2,6-linked sialic acids and lactonization of α2,3-linked variants, in short time using mild conditions. Glycans were recovered by hydrophilic interaction liquid chromatography solid phase extraction and analyzed by MALDI-TOF-MS in reflectron positive mode with 2,5-dihydroxybenzoic acid as the matrix substance. Analysis of the human plasma N-glycome allowed high-throughput detection and relative quantitation of more than 100 distinct N-glycan compositions with varying sialic acid linkages.

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Metadata

Authors
Reiding, K. R., Blank, D., Kuijper, D. M., Deelder, A. M., & Wuhrer, M.
Venue
Analytical Chemistry
Publisher
American Chemical Society (ACS)
Published
2014-05-28
Volume
86
Issue
12
Pages
5784-5793
ISSN
  • 0003-2700 (ISSN-L)
  • 1520-6882
DOI
10.1021/ac500335t
OpenAlex
W2321180610
Cited by
334
References
43
FWCI
12.53
Type
journal article
Language
en
Open access
closed

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