Journal
ANALYTICAL AND BIOANALYTICAL CHEMISTRY
Volume 409, Issue 18, Pages 4437-4447Publisher
SPRINGER HEIDELBERG
DOI: 10.1007/s00216-017-0387-6
Keywords
Glycomics; N-Glycans; MALDI imaging; Quantitation; HILIC; Hydrazide reagents
Funding
- National Institutes of Health (NIH) [R21AG055377, R01 DK071801, R56 MH110215]
- NIH shared instrument grant [NIH-NCRR S10RR029531]
- Office of the Vice Chancellor for Research and Graduate Education at the University of Wisconsin- Madison
- Wisconsin Alumni Research Foundation
- University of Wisconsin- Madison School of Pharmacy
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In this work, the capability of newly developed hydrophilic interaction liquid chromatography (HILIC) coupled with matrix-assisted laser desorption/ionization-mass spectrometric imaging (MALDI-MSI) platform for quantitative analysis of N-glycans has been demonstrated. As a proof-of-principle experiment, heavy and light stable-isotope labeled hydrazide reagents labeled maltodextrin ladder were used to demonstrate the feasibility of the HILIC-MALDI-MSI platform for reliable quantitative analysis of N-glycans. MALDI-MSI analysis by an Orbitrap mass spectrometer enabled high-resolution and high-sensitivity detection of N-glycans eluted from HILIC column, allowing the re-construction of LC chromatograms as well as accurate mass measurements for structural inference. MALDI-MSI analysis of the collected LC traces showed that the chromatographic resolution was preserved. The N-glycans released from human serum was used to demonstrate the utility of this novel platform in quantitative analysis of N-glycans from a complex sample. Benefiting from the minimized ion suppression provided by HILIC separation, comparison between MALDI-MS and the newly developed platform HILIC-MALDI-MSI revealed that HILIC-MALDI-MSI provided higher N-glycan coverage as well as better quantitation accuracy in the quantitative analysis of N-glycans released from human serum.
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