Dataset Information

Radical-directed dissociation of peptides and proteins by infrared multiphoton dissociation and sustained off-resonance irradiation collision-induced dissociation with Fourier transform ion cyclotron resonance mass spectrometry.

ABSTRACT: Recent experiments utilizing photodissociation in linear ion traps have enabled significant development of Radical-Directed Dissociation (RDD) for the examination of peptides and proteins. The increased mass accuracy and resolution available in Fourier transform ion cyclotron resonance mass spectrometry (FTICR-MS) should enable further progress in this area. Preliminary experiments with photoactivated radicals are reported herein.A 266 nm Nd:YAG laser is coupled to a FTICR or linear ion trap mass spectrometer. Radical peptides and proteins are generated by ultraviolet photodissociation (PD) and further activated by collisions or infrared photons.A 266 nm UV laser and an IR laser can be simultaneously coupled to a 15 Tesla FTICR mass spectrometer. The ultra-low-pressure environment in FTICR-MS makes collisional cooling less competitive, and thus more secondary fragments are generated by UVPD than in linear ion traps. Activation by sustained off-resonance irradiation collision-induced dissociation (SORI-CID) or infrared multiphoton dissociation (IRMPD) also yields additional secondary fragmentation relative to CID in an ion trap. Accurate identification of RDD fragments is possible in FTICR-MS.Relative to linear ion trap instruments, PD experiments in FTICR-MS are more difficult to execute due to poor ion cloud overlap and the low pressure environment. However, the results can be more easily interpreted due to the increased resolution and mass accuracy.

SUBMITTER: Zhang X

PROVIDER: S-EPMC4237167 | biostudies-literature | 2014 Dec

REPOSITORIES: biostudies-literature

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Radical-directed dissociation of peptides and proteins by infrared multiphoton dissociation and sustained off-resonance irradiation collision-induced dissociation with Fourier transform ion cyclotron resonance mass spectrometry.

Zhang Xing X Li Huilin H Moore Benjamin B Wongkongkathep Piriya P Ogorzalek Loo Rachel R RR Loo Joseph A JA Julian Ryan R RR

Rapid communications in mass spectrometry : RCM 20141201 24

<h4>Rationale</h4>Recent experiments utilizing photodissociation in linear ion traps have enabled significant development of Radical-Directed Dissociation (RDD) for the examination of peptides and proteins. The increased mass accuracy and resolution available in Fourier transform ion cyclotron resonance mass spectrometry (FTICR-MS) should enable further progress in this area. Preliminary experiments with photoactivated radicals are reported herein.<h4>Methods</h4>A 266 nm Nd:YAG laser is coupled ...[more]

PMID: 25380495

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Project description:Metabolomics is an interdisciplinary field that aims to study all metabolites < 1500 Da that are ubiquitously found within all organisms. Metabolomics is experiencing exponential growth and commonly relies on high-resolution mass spectrometry (HRMS). Fourier transform ion cyclotron resonance mass spectrometry (FT-ICR-MS) is a form of HRMS that is particularly well suited for metabolomics research due to its exceptionally high resolution (105-106) and sensitivity with a mass accuracy in parts per billion (ppb). In this regard, FT-ICR-MS can provide valuable insights into the metabolomics analysis of complex biological systems due to unique capabilities such as the easy separation of isobaric and isomeric species, isotopic fine structure analysis, spatial resolution of metabolites in cells and tissues, and a high confidence (<1 ppm mass error) in metabolite identification. Alternatively, the large and complex data sets, long acquisition times, high cost, and limited access mainly through national mass spectrometry facilities may impede the routine adoption of FT-ICR-MS by metabolomics researchers. This review examines recent applications of FT-ICR-MS metabolomics in the search for clinical and non-human biomarkers; for the analysis of food, beverage, and environmental samples; and for the high-resolution imaging of tissues and other biological samples. We provide recent examples of metabolomics studies that highlight the advantages of FT-ICR-MS for the detailed and reliable characterization of the metabolome. Additionally, we offer some practical considerations for implementing FT-ICR-MS into a research program by providing a list of FT-ICR-MS facilities and by identifying different high-throughput interfaces, varieties of sample types, analysis methods (e.g., van Krevelen diagrams, Kendrick mass defect plot, etc.), and sample preparation and handling protocols used in FT-ICR-MS experiments. Overall, FT-ICR-MS holds great promise as a vital research tool for advancing metabolomics investigations.

Dataset Information

Radical-directed dissociation of peptides and proteins by infrared multiphoton dissociation and sustained off-resonance irradiation collision-induced dissociation with Fourier transform ion cyclotron resonance mass spectrometry.

Publications

Radical-directed dissociation of peptides and proteins by infrared multiphoton dissociation and sustained off-resonance irradiation collision-induced dissociation with Fourier transform ion cyclotron resonance mass spectrometry.

Similar Datasets

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