2020
DOI: 10.1021/acs.analchem.0c03412
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Enhancing Top-Down Analysis Using Chromophore-Assisted Infrared Multiphoton Dissociation from (Phospho)peptides to Protein Assemblies

Abstract: Infrared multiphoton dissociation (IRMPD) has been used in mass spectrometry to fragment peptides and proteins, providing fragments mostly similar to collisional activation. Using the 10.6 μm wavelength of a CO2 laser, IRMPD suffers from the relative low absorption cross-section of peptides and small proteins. Focusing on top-down analysis, we investigate different means to tackle this issue. We first reassess efficient sorting of phosphopeptides from nonphosphopeptides based on IR-absorption cross-sectional e… Show more

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Cited by 18 publications
(29 citation statements)
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“…Particularly large protein assemblies measured at high m / z can therefore benefit from the development of alternative desolvation methods that are less charge-state-dependent. Recent work demonstrated that in particular IRMPD could also be used to enhance desolvation, possibly even more effectively than CID, and should therefore possibly be more explored for native MS …”
Section: Tandem Mass Spectrometry and Ion Activation In Native Msmentioning
confidence: 99%
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“…Particularly large protein assemblies measured at high m / z can therefore benefit from the development of alternative desolvation methods that are less charge-state-dependent. Recent work demonstrated that in particular IRMPD could also be used to enhance desolvation, possibly even more effectively than CID, and should therefore possibly be more explored for native MS …”
Section: Tandem Mass Spectrometry and Ion Activation In Native Msmentioning
confidence: 99%
“…In addition, IRMPD provides a high level of control over the amount of energy deposited by photon irradiation. These advantages prompted researchers to implement IRMPD on the various instruments used for native MS, including Q-ToF-, FT-ICR-, and Orbitrap-based instruments . The groups of Loo and Gross have extensively explored the application of IRMPD for native top-down MS on ICR platforms, primarily using this method for supplemental activation of proteins and protein complexes along with fragmentation using more energetic and prompt activation techniques like ECD.…”
Section: Tandem Mass Spectrometry and Ion Activation In Native Msmentioning
confidence: 99%
See 1 more Smart Citation
“…Here, we aim at analyzing these very large and important, albeit structurally complicated, oligomeric immunoglobulins, through the application of native top-down mass spectrometry (nTDMS). Relying on the fact that native MS transfers the molecules to the gas phase under conditions retaining their structural features, native top-down proteomics should provide access to the sequence of the proteins’ subunits and an insight into its post-translational modifications and higher-order structure. It has become apparent that inducing fragmentation in native top-down proteomics requires moving beyond the well-established activation method of collision-induced dissociation (CID) as this rather slow heating process often induces too little fragmentation when applied to these very high mass systems. Several groups have explored alternative fragmentation methods for nTDMS, such as surface-induced dissociation, photon-induced dissociation (UVPD and IRMPD), electron transfer dissociation, , and electron capture dissociation (ECD). ,,, …”
Section: Introductionmentioning
confidence: 99%
“…The dissociation of gaseous ions in tandem mass spectrometry requires the deposition of sufficient internal energy into the target ions, which can be achieved by collisions with neutral molecules or suitable surfaces, capture or transformation of electrons, reaction with radicals, or photon excitation. In the last case, both infrared (IR) and ultraviolet (UV) lasers have been applied. For infrared multiphoton dissociation (IRMPD), the internal energy of the target ion increases in multiple steps until it reaches the threshold energy for dissociation. When tunable IR lasers are applied in such experiments, the IRMPD action spectra of the target ions are typically obtained by monitoring the dissociation of the precursor ions as a function of the applied wavelength. Ultraviolet photodissociation (UVPD) has garnered significant interest in recent years. Single-wavelength UV lasers, such as 266, 213, and 193 nm lasers, have been widely applied in mass spectrometric studies for the analysis of organic and biological molecules. Extreme UV radiation has even been applied as an efficient method for ion activation and dissociation .…”
mentioning
confidence: 99%