scholarly journals Biologically relevant metal-cation binding induces conformational changes in heparin oligosaccharides as measured by ion mobility mass spectrometry

2011 ◽  
Vol 303 (2-3) ◽  
pp. 191-198 ◽  
Author(s):  
Youjin Seo ◽  
Matthew R. Schenauer ◽  
Julie A. Leary
Keyword(s):  
Mass Spectrometry ◽  
Conformational Changes ◽  
Ion Mobility ◽  
Metal Cation ◽  
Cation Binding ◽  
Ion Mobility Mass Spectrometry ◽  
Biologically Relevant ◽  
Heparin Oligosaccharides

Ion mobility mass spectrometry workflows for characterizing bioactive isomer conformation, isomerization and drug–protein–liposome interaction

2018 ◽  
Vol 10 (36) ◽  
pp. 4367-4377
Author(s):  
Hui Ouyang ◽  
Tao Bo ◽  
Zhengxiang Zhang ◽  
Xinqiu Guo ◽  
Mingzhen He ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Conformational Changes ◽  
Ion Mobility ◽  
Ion Mobility Mass Spectrometry

Ion mobility mass spectrometry enhances our ability to study conformational changes of bioactive isomers and their interactions with macromolecules.

Exploring Key Parameters to Detect Subtle Ligand-Induced Protein Conformational Changes Using Traveling Wave Ion Mobility Mass Spectrometry

2012 ◽  
Vol 84 (11) ◽  
pp. 4703-4710 ◽  
Author(s):  
Cédric Atmanene ◽  
Stéphanie Petiot-Bécard ◽  
Denis Zeyer ◽  
Alain Van Dorsselaer ◽  
Valérie Vivat Hannah ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Conformational Changes ◽  
Ion Mobility ◽  
Traveling Wave ◽  
Ion Mobility Mass Spectrometry ◽  
Protein Conformational Changes ◽  
Traveling Wave Ion Mobility

scholarly journals Ion mobility coupled to native mass spectrometry as a relevant tool to investigate extremely small ligand-induced conformational changes

The Analyst ◽  
2015 ◽  
Vol 140 (21) ◽  
pp. 7234-7245 ◽  
Author(s):  
Johann Stojko ◽  
Sonia Fieulaine ◽  
Stéphanie Petiot-Bécard ◽  
Alain Van Dorsselaer ◽  
Thierry Meinnel ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Conformational Changes ◽  
Ion Mobility ◽  
Native Mass Spectrometry ◽  
Peptide Deformylase ◽  
Ion Mobility Mass Spectrometry ◽  
Over Time

Native and ion-mobility mass spectrometry reveal the conformational evolution over time of a peptide deformylase binding different ligands, which is consistent with slow-tight inhibition of the enzyme.

scholarly journals Alkali metal cation adduct effect on polybutylene adipate oligomers: Ion mobility-mass spectrometry

Polymer ◽  
2019 ◽  
Vol 173 ◽  
pp. 58-65 ◽  
Author(s):  
Tiffany M. Crescentini ◽  
Jody C. May ◽  
John A. McLean ◽  
David M. Hercules
Keyword(s):  
Mass Spectrometry ◽  
Alkali Metal ◽  
Ion Mobility ◽  
Metal Cation ◽  
Alkali Metal Cation ◽  
Ion Mobility Mass Spectrometry

Ion Mobility—Mass Spectrometry-Based Screening for Inhibition of α-Synuclein Aggregation

2015 ◽  
Vol 21 (3) ◽  
pp. 255-264 ◽  
Author(s):  
Yanqin Liu ◽  
Michael Graetz ◽  
Lam Ho ◽  
Tara L. Pukala
Keyword(s):  
Mass Spectrometry ◽  
Conformational Changes ◽  
Ion Mobility ◽  
Amyloid Fibrils ◽  
Therapeutic Agents ◽  
Ion Mobility Mass Spectrometry ◽  
Amyloid Formation ◽  
Protein Ligand Interactions ◽  
Ligand Interactions ◽  
Screening Approaches

Aberrant protein folding and formation of amyloid fibrils are associated with numerous debilitating human diseases, for which there are currently no suitable therapeutic treatments. For instance, Parkinson's disease is characterised pathologically by the intraneural accumulation of the amyloid protein α-synuclein. In order to search for new therapeutic agents that are effective in preventing the early conformational changes that precede protein aggregation, it is necessary to devise new analytical screening approaches. Here we demonstrate the use of ion mobility–mass spectrometry for screening of molecules capable of inhibiting the misfolding and aggregation of α-synuclein (specifically, the A53T human mutant). Importantly, this assay allows for the analysis of conformational changes that precede aggregation, and therefore is unique in its ability to identify inhibitors working at the earliest stages of amyloid formation. In addition, we use complementary mass spectrometry methods to probe selected protein–ligand interactions responsible for fibril inhibition.

Rapid Diagnosis of Parkinson’s Disease from Sebum using Paper Spray Ionisation Ion Mobility Mass Spectrometry

2020 ◽  
Author(s):  
Depanjan Sarkar ◽  
Drupad Trivedi ◽  
Eleanor Sinclair ◽  
Sze Hway Lim ◽  
Caitlin Walton-Doyle ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Parkinson’S Disease ◽  
Parkinson's Disease ◽  
Ion Mobility ◽  
Neurodegenerative Disorder ◽  
Treatment Options ◽  
Ion Mobility Mass Spectrometry ◽  
Paper Spray ◽  
Molecular Features ◽  
Validation Set

Parkinson’s disease (PD) is the second most common neurodegenerative disorder for which identification of robust biomarkers to complement clinical PD diagnosis would accelerate treatment options and help to stratify disease progression. Here we demonstrate the use of paper spray ionisation coupled with ion mobility mass spectrometry (PSI IM-MS) to determine diagnostic molecular features of PD in sebum. PSI IM-MS was performed directly from skin swabs, collected from 34 people with PD and 30 matched control subjects as a training set and a further 91 samples from 5 different collection sites as a validation set. PSI IM-MS elucidates ~ 4200 features from each individual and we report two classes of lipids (namely phosphatidylcholine and cardiolipin) that differ significantly in the sebum of people with PD. Putative metabolite annotations are obtained using tandem mass spectrometry experiments combined with accurate mass measurements. Sample preparation and PSI IM-MS analysis and diagnosis can be performed ~5 minutes per sample offering a new route to for rapid and inexpensive confirmatory diagnosis of this disease.

Sign in / Sign up

Export Citation Format

Share Document