Separation and Identification of Isomeric Glycans by Selected Accumulation-Trapped Ion Mobility Spectrometry-Electron Activated Dissociation Tandem Mass Spectrometry
Author(s) -
Yi Pu,
Mark E. Ridgeway,
Rebecca S. Glaskin,
Melvin A. Park,
Catherine E. Costello,
Cheng Lin
Publication year - 2016
Publication title -
analytical chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.117
H-Index - 332
eISSN - 1520-6882
pISSN - 0003-2700
DOI - 10.1021/acs.analchem.6b00041
Subject(s) - chemistry , fourier transform ion cyclotron resonance , mass spectrometry , tandem mass spectrometry , ion mobility spectrometry , electron capture dissociation , glycan , top down proteomics , dissociation (chemistry) , collision induced dissociation , analytical chemistry (journal) , ion , tandem , protein mass spectrometry , chromatography , organic chemistry , biochemistry , materials science , glycoprotein , composite material
One of the major challenges in structural characterization of oligosaccharides is the presence of many structural isomers in most naturally occurring glycan mixtures. Although ion mobility spectrometry (IMS) has shown great promise in glycan isomer separation, conventional IMS separation occurs on the millisecond time scale, largely restricting its implementation to fast time-of-flight (TOF) analyzers which often lack the capability to perform electron activated dissociation (ExD) tandem MS analysis and the resolving power needed to resolve isobaric fragments. The recent development of trapped ion mobility spectrometry (TIMS) provides a promising new tool that offers high mobility resolution and compatibility with high-performance Fourier transform ion cyclotron resonance (FTICR) mass spectrometers when operated under the selected accumulation-TIMS (SA-TIMS) mode. Here, we present our initial results on the application of SA-TIMS-ExD-FTICR MS to the separation and identification of glycan linkage isomers.
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