Increasing the hydrophobicity and electrospray response of glycans through derivatization with novel cationic hydrazides

Bereman, Michael S.; Comins, Daniel L.; Muddiman, David C.

doi:10.1039/b915589a

Cited by 53 publications

(68 citation statements)

References 20 publications

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“…Researchers have been hesitant to incorporate a permanent charge hypothesizing that it would have a negative effect in the fragmentation patterns of the glycans and could cause partial or total loss of the tag 18 . Recently, though, it has been shown that CID fragmentation patterns of a charged complex glycan are not negatively affected by a permanently charged tag nor is the tag lost during fragmentation 29 . Given these results, charged hydrazide reagents are now considered a viable avenue toward the hydrophobic tagging of glycans.…”

Section: Introductionmentioning

confidence: 99%

Interplay of Permanent Charge and Hydrophobicity in the Electrospray Ionization of Glycans

et al. 2010

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The analysis of N-linked glycans by mass spectrometry (MS) has been characterized by low signal-to-noise ratios and high limits of detection due to their hydrophilicity and lack of basic sites able to be protonated. As a result, every step in glycan sample preparation must be thoroughly optimized in order to minimize sample loss, contamination, and analytical variability. Importantly, properties of glycans and their derivatized counterparts must be thoroughly studied in order to exploit certain characteristics for enhancing MS analysis. Herein, the effectiveness of the incorporation of a permanent charge is studied and determined to hamper glycan analysis. Also, a procedure for glycan hydrazone formation is optimized and outlined where a large number of variables were simultaneously analyzed using a fractional factorial design (FFD) in order to determine which conditions affected the reaction efficiency of the hydrazone formation reaction. Finally, the hydrophobic tagging of glycans is shown to be a viable opportunity to further increase the ion abundance of glycans in MS.

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Section: Introductionmentioning

confidence: 99%

Interplay of Permanent Charge and Hydrophobicity in the Electrospray Ionization of Glycans

et al. 2010

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“…Two related derivatives prepared from the 4-phenyl pyridine (108) and the tripropylamino-analogue of Girard's T reagent (109) have been prepared and examined by HILIC nano-LC/MS [248]. Both derivatives but particularly the tripropylamino-analogue, produced an increase in sensitivity but, unlike the earlier reports, the sensitivity of the Girard's T derivative of maltoheptaose was lower that that from the unlabelled carbohydrate.…”

Section: Hydrazonesmentioning

confidence: 94%

Derivatization of carbohydrates for analysis by chromatography; electrophoresis and mass spectrometry

Harvey¹

2011

Journal of Chromatography B

217

156

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“…Hydrophobic tagging has demonstrated great potential to dramatically increase the utility of MS-based proteomics by improving the detectability of derivatized peptides and proteins and, more recently, has even shown promise for the ana lysis of glycans [33,34]. However, based on the studies to date, it is clear that no universal reagent exists that will positively impact the characterization of an entire proteome and, thus, future applications of hydrophobic tagging are expected to remain focused on targeted analyses for which an optimal reagent can be determined.…”

Section: Five-year Viewmentioning

confidence: 99%

Capitalizing on the hydrophobic bias of electrospray ionization through chemical modification in mass spectrometry-based proteomics

Shuford

Muddiman

2011

Expert Review of Proteomics

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Protein chemical derivatization has emerged as an invaluable bioanalytical approach in mass spectrometry-based proteomics with nearly unlimited potential. To date, derivatization strategies in proteomics have primarily focused on improving mass spectral identification and relative quantification of proteins, as well as increasing enrichment yield from complex mixtures. However, there is a great opportunity to develop and exploit front-end chemical processes to enhance the ability to detect low-abundant peptides and proteins for a large number of applications. The content of this article focuses on improvements in targeted, mass spectrometry-based proteomic strategies, achieved by taking advantage of the mechanism of ESI through the use of hydrophobic chemical derivatization.

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Increasing the hydrophobicity and electrospray response of glycans through derivatization with novel cationic hydrazides

Abstract: Novel tags are used to increase the hydrophobicity of glycans and impart a permanent charge yielding as great as a approximately 5-fold increase in electrospray response from both a standard and complex mixture.

Cited by 53 publications

References 20 publications

Interplay of Permanent Charge and Hydrophobicity in the Electrospray Ionization of Glycans

Interplay of Permanent Charge and Hydrophobicity in the Electrospray Ionization of Glycans

Derivatization of carbohydrates for analysis by chromatography; electrophoresis and mass spectrometry

Capitalizing on the hydrophobic bias of electrospray ionization through chemical modification in mass spectrometry-based proteomics

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