scholarly journals Comparison of ion mobility-mass spectrometry and pulsed-field gradient nuclear magnetic resonance spectroscopy for the differentiation of chondroitin sulfate isomers

2016 ◽  
Vol 8 (48) ◽  
pp. 8483-8491 ◽  
Author(s):  
Katharina Lemmnitzer ◽  
Thomas Riemer ◽  
Michael Groessl ◽  
Rosmarie Süβ ◽  
Richard Knochenmuss ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Nuclear Magnetic Resonance ◽  
Chondroitin Sulfate ◽  
Field Gradient ◽  
Ion Mobility ◽  
Enzymatic Digestion ◽  
Resonance Spectroscopy ◽  
Ion Mobility Mass Spectrometry ◽  
Pulsed Field ◽  
Unsaturated Disaccharide

The unsaturated disaccharide isomers of chondroitin sulfate (CS) obtained by enzymatic digestion of the polysaccharide can be differentiated in mixtures by ion mobility MS (A) as well as pulsed-field gradient NMR (B).

scholarly journals Correlating glycoforms of DC-SIGN with stability using a combination of enzymatic digestion and ion mobility MS

2020 ◽  
Author(s):  
Hsin-Yung Yen ◽  
Idlir Liko ◽  
Joseph Gault ◽  
Di Wu ◽  
Weston B. Struwe ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Gas Phase ◽  
Ion Mobility ◽  
Collision Cross Section ◽  
Enzymatic Digestion ◽  
Ion Mobility Mass Spectrometry ◽  
Structural Detail ◽  
The Core ◽  
Glycosylation Sites ◽  
The Stability

AbstractThe immune scavenger protein DC-SIGN interacts with glycosylated proteins and has a putative role in facilitating viral infection. How these recognition events take place with different viruses is not clear and the effects of glycosylation on the folding and stability of DC-SIGN have not been reported. Here, we develop and apply a mass spectrometry-based approach to both uncover and characterise the effects of O-glycans on the stability of DC-SIGN. We first quantify the Core 1 & 2 O-glycan structures on the carbohydrate recognition and extracellular domains of the protein via sequential exoglycosidase sequencing. We then use ion mobility mass spectrometry to show how specific O-glycans, and/or single monosaccharide substitutions, alter both the overall collision cross section and the gas-phase stability of the glycoprotein isoforms of DC-SIGN. We find that rather than the mass or length of glycoprotein modifications, the stability of DC-SIGN is better correlated with the number of glycosylation sites. Collectively, our results exemplify a combined multi-dimensional MS approach, proficient in evaluating protein stability in response to both glycoprotein macro- and micro-heterogeneity and adding structural detail to the infection enhancer DC-SIGN.

scholarly journals Correlating Glycoforms of DC‐SIGN with Stability Using a Combination of Enzymatic Digestion and Ion Mobility Mass Spectrometry

2020 ◽  
Vol 59 (36) ◽  
pp. 15560-15564
Author(s):  
Hsin‐Yung Yen ◽  
Idlir Liko ◽  
Joseph Gault ◽  
Di Wu ◽  
Weston B. Struwe ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Ion Mobility ◽  
Enzymatic Digestion ◽  
Ion Mobility Mass Spectrometry
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