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1. Coupling trapped ion mobility spectrometry to mass spectrometry: trapped ion mobility spectrometry-time-of-flight mass spectrometry versus trapped ion mobility spectrometry-Fourier transform ion cyclotron resonance mass spectrometry

   https://doi.org/10.1002/rcm.8165  

   Tose, Lilian V.; Benigni, Paolo; Leyva, Dennys; Sundberg, Abigail; Ramírez, César E.; Ridgeway, Mark E.; Park, Melvin A.; Romão, Wanderson; Jaffé, Rudolf; Fernandez-Lima, Francisco (August 2018, Rapid Communications in Mass Spectrometry)
2. Effective Liquid Chromatography–Trapped Ion Mobility Spectrometry–Mass Spectrometry Separation of Isomeric Lipid Species

   https://doi.org/10.1021/acs.analchem.8b04979  

   Jeanne Dit Fouque, Kevin; Ramirez, Cesar E.; Lewis, Russell L.; Koelmel, Jeremy P.; Garrett, Timothy J.; Yost, Richard A.; Fernandez-Lima, Francisco (February 2019, Analytical Chemistry)
3. Identification of Lasso Peptide Topologies Using Native Nanoelectrospray Ionization-Trapped Ion Mobility Spectrometry–Mass Spectrometry

   https://doi.org/10.1021/acs.analchem.7b05230  

   Dit Fouque, Kevin Jeanne; Moreno, Javier; Hegemann, Julian D.; Zirah, Séverine; Rebuffat, Sylvie; Fernandez-Lima, Francisco (April 2018, Analytical Chemistry)
4. Tandem‐trapped ion mobility spectrometry/mass spectrometry coupled with ultraviolet photodissociation

   https://doi.org/10.1002/rcm.9192  

   Liu, Fanny_C; Ridgeway, Mark_E; Winfred, J_S_Raaj_Vellore; Polfer, Nicolas_C; Lee, Jusung; Theisen, Alina; Wootton, Christopher_A; Park, Melvin_A; Bleiholder, Christian (September 2021, Rapid Communications in Mass Spectrometry)

   RationaleTandem‐ion mobility spectrometry/mass spectrometry methods have recently gained traction for the structural characterization of proteins and protein complexes. However, ion activation techniques currently coupled with tandem‐ion mobility spectrometry/mass spectrometry methods are limited in their ability to characterize structures of proteins and protein complexes. MethodsHere, we describe the coupling of the separation capabilities of tandem‐trapped ion mobility spectrometry/mass spectrometry (tTIMS/MS) with the dissociation capabilities of ultraviolet photodissociation (UVPD) for protein structure analysis. ResultsWe establish the feasibility of dissociating intact proteins by UV irradiation at 213 nm between the two TIMS devices in tTIMS/MS and at pressure conditions compatible with ion mobility spectrometry (2–3 mbar). We validate that the fragments produced by UVPD under these conditions result from a radical‐based mechanism in accordance with prior literature on UVPD. The data suggest stabilization of fragment ions produced from UVPD by collisional cooling due to the elevated pressures used here (“UVnoD2”), which otherwise do not survive to detection. The data account for a sequence coverage for the protein ubiquitin comparable to recent reports, demonstrating the analytical utility of our instrument in mobility‐separating fragment ions produced from UVPD. ConclusionsThe data demonstrate that UVPD carried out at elevated pressures of 2–3 mbar yields extensive fragment ions rich in information about the protein and that their exhaustive analysis requires IMS separation post‐UVPD. Therefore, because UVPD and tTIMS/MS each have been shown to be valuable techniques on their own merit in proteomics, our contribution here underscores the potential of combining tTIMS/MS with UVPD for structural proteomics. 

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5. Dynamic mass spectrometry probe for electrospray ionization mass spectrometry monitoring of bioreactors for therapeutic cell manufacturing

   https://doi.org/10.1002/bit.26832  

   Chilmonczyk, Mason_A; Kottke, Peter_A; Stevens, Hazel_Y; Guldberg, Robert_E; Fedorov, Andrei_G (November 2018, Biotechnology and Bioengineering)

   Abstract Large‐scale manufacturing of therapeutic cells requires bioreactor technologies with online feedback control enabled by monitoring of secreted biomolecular critical quality attributes (CQAs). Electrospray ionization mass spectrometry (ESI‐MS) is a highly sensitive label‐free method to detect and identify biomolecules, but requires extensive sample preparation before analysis, making online application of ESI‐MS challenging. We present a microfabricated, monolithically integrated device capable of continuous sample collection, treatment, and direct infusion for ESI‐MS detection of biomolecules in high‐salt solutions. The dynamic mass spectrometry probe (DMSP) uses a microfluidic mass exchanger to rapidly condition samples for online MS analysis by removing interfering salts, while concurrently introducing MS signal enhancers to the sample for sensitive biomolecular detection. Exploiting this active conditioning capability increases MS signal intensity and signal‐to‐noise ratio. As a result, sensitivity for low‐concentration biomolecules is significantly improved, and multiple proteins can be detected from chemically complex samples. Thus, the DMSP has significant potential to serve as an enabling portion of a novel analytical tool for discovery and monitoring of CQAs relevant to therapeutic cell manufacturing. 

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