NDLI: It is all about the solvent: on the importance of the mobile phase for ZIC-HILIC glycopeptide enrichment

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It is all about the solvent: on the importance of the mobile phase for ZIC-HILIC glycopeptide enrichment

Content Provider	Springer Nature Link
Author	Alagesan, Kathirvel Khilji, Sana Khan Kolarich, Daniel
Copyright Year	2016
Abstract	Glycopeptide enrichment is a crucial step in glycoproteomics for which hydrophilic interaction chromatography (HILIC) has extensively been applied due to its low bias towards different glycan types. A systematic evaluation of applicable HILIC mobile phases on glycopeptide enrichment efficiency and selectivity is, to date, however, still lacking. Here, we present a novel, simplified technique for HILIC enrichment termed “Drop-HILIC”, which was applied to systematically evaluate the mobile phase effect on ZIC-HILIC (zwitterionic type of hydrophilic interaction chromatography) glycopeptide enrichment. The four most commonly used MS compatible organic solvents were investigated: (i) acetonitrile, (ii) methanol, (iii) ethanol and (iv) isopropanol. Glycopeptide enrichment efficiencies were evaluated for each solvent system using samples of increasing complexity ranging from well-defined synthetic glycopeptides spiked into different concentrations of tryptic BSA peptides, followed by standard glycoproteins, and a complex sample derived from human (depleted and non-depleted) serum. ZIC-HILIC glycopeptide efficiency largely relied upon the used solvent. Different organic mobile phases enriched distinct glycopeptide subsets in a peptide backbone hydrophilicity-dependant manner. Acetonitrile provided the best compromise for the retention of both hydrophilic and hydrophobic glycopeptides, whereas methanol was confirmed to be unsuitable for this purpose. The enrichment efficiency of ethanol and isopropanol towards highly hydrophobic glycopeptides was compromised as considerable co-enrichment of unmodified peptides occurred, though for some hydrophobic glycopeptides isopropanol showed the best enrichment properties. This study shows that even minor differences in the peptide backbone and solvent do significantly influence HILIC glycopeptide enrichment and need to be carefully considered when employed for glycopeptide enrichment. Graphical Abstract The organic solvent plays a crucial role in ZIC-HILIC glycopeptide enrichment
Starting Page	529
Ending Page	538
Page Count	10
File Format	PDF
ISSN	16182642
Journal	Analytical and Bioanalytical Chemistry
Volume Number	409
Issue Number	2
e-ISSN	16182650
Language	English
Publisher	Springer Berlin Heidelberg
Publisher Date	2016-12-01
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Glycoproteomics Glycopeptide enrichment Hydrophilic interaction chromatography HILIC Glycopeptide synthesis Analytical Chemistry Biochemistry Laboratory Medicine Characterization and Evaluation of Materials Food Science Monitoring/Environmental Analysis
Content Type	Text
Resource Type	Article
Subject	Analytical Chemistry Biochemistry

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It is all about the solvent: on the importance of the mobile phase for ZIC-HILIC glycopeptide enrichment

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It is all about the solvent: on the importance of the mobile phase for ZIC-HILIC glycopeptide enrichment

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It is all about the solvent: on the importance of the mobile phase for ZIC-HILIC glycopeptide enrichment