scholarly journals Targeted High-Resolution Ion Mobility Separation Coupled to Ultrahigh-Resolution Mass Spectrometry of Endocrine Disruptors in Complex Mixtures

2015 ◽  
Vol 87 (8) ◽  
pp. 4321-4325 ◽  
Author(s):  
Paolo Benigni ◽  
Christopher J. Thompson ◽  
Mark E. Ridgeway ◽  
Melvin A. Park ◽  
Francisco Fernandez-Lima
Keyword(s):  
Mass Spectrometry ◽  
High Resolution ◽  
Endocrine Disruptors ◽  
Ion Mobility ◽  
Complex Mixtures ◽  
Ultrahigh Resolution ◽  
Mobility Separation ◽  
Ion Mobility Separation ◽  
Resolution Mass

Spatial Metabolomics of the Human Kidney Using MALDI Trapped Ion Mobility Imaging Mass Spectrometry

2020 ◽  
Author(s):  
Elizabeth Neumann ◽  
Lukasz Migas ◽  
Jamie L. Allen ◽  
Richard Caprioli ◽  
Raf Van de Plas ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Ion Mobility ◽  
Imaging Mass Spectrometry ◽  
Structural Complexity ◽  
Human Kidney ◽  
Resolving Power ◽  
Mobility Separation ◽  
Trapped Ion ◽  
Mobility Data ◽  
Ion Mobility Separation

<div> <div> <p>Small metabolites are essential for normal and diseased biological function but are difficult to study because of their inherent structural complexity. MALDI imaging mass spectrometry (IMS) of small metabolites is particularly challenging as MALDI matrix clusters are often isobaric with metabolite ions, requiring high resolving power instrumentation or derivatization to circumvent this issue. An alternative to this is to perform ion mobility separation before ion detection, enabling the visualization of metabolites without the interference of matrix ions. Here, we use MALDI timsTOF IMS to image small metabolites at high spatial resolution within the human kidney. Through this, we have found metabolites, such as arginic acid, acetylcarnitine, and choline that localize to the cortex, medulla, and renal pelvis, respectively. We have also demonstrated that trapped ion mobility spectrometry (TIMS) can resolve matrix peaks from metabolite signal and separate both isobaric and isomeric metabolites with different localizations within the kidney. The added ion mobility data dimension dramatically increased the peak capacity for molecular imaging experiments. Future work will involve further exploring the small metabolite profiles of human kidneys as a function of age, gender, and ethnicity.</p></div></div>

scholarly journals N-Glycosylation profiling of intact target proteins by high-resolution mass spectrometry (MS) and glycan analysis using ion mobility-MS/MS

The Analyst ◽  
2020 ◽  
Vol 145 (5) ◽  
pp. 1737-1748
Author(s):  
Alessandro Quaranta ◽  
Maya Spasova ◽  
Elena Passarini ◽  
Isabella Karlsson ◽  
Lorena Ndreu ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Quality Control ◽  
High Resolution ◽  
Ion Mobility ◽  
High Resolution Mass Spectrometry ◽  
Target Proteins ◽  
Intact Proteins ◽  
Glycan Analysis ◽  
High Resolution Mass ◽  
Resolution Mass

Glycosylation characterization could lead to the discovery of biomarkers and is crucial in quality control of biopharmaceuticals. Here we present a method to quantify glycoforms on intact proteins, with parallel glycan identification by IMS-MS/MS.

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