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Generation and detection of multiply-charged peptides and proteins by matrix-assisted laser desorption electrospray ionization (MALDESI) fourier transform ion cyclotron resonance mass spectrometry
Author(s) -
Jason S. Sampson,
Adam M. Hawkridge,
David C. Muddiman
Publication year - 2006
Publication title -
journal of the american society for mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.961
H-Index - 127
eISSN - 1879-1123
pISSN - 1044-0305
DOI - 10.1016/j.jasms.2006.08.003
Subject(s) - fourier transform ion cyclotron resonance , chemistry , mass spectrometry , electrospray ionization , ionization , ion source , analytical chemistry (journal) , ion cyclotron resonance , ambient ionization , matrix assisted laser desorption/ionization , top down proteomics , desorption electrospray ionization , matrix assisted laser desorption electrospray ionization , protein mass spectrometry , electrospray , time of flight mass spectrometry , maldi imaging , atmospheric pressure laser ionization , ion , desorption , photoionization , chemical ionization , chromatography , electron ionization , cyclotron , organic chemistry , adsorption
We report the coupling of a hybrid ionization source, matrix-assisted laser desorption electrospray ionization (MALDESI), to a Fourier transform-ion cyclotron resonance mass spectrometer (FT-ICR MS). The details of the source design and initial data are presented. Analysis of peptides and proteins ranging from 1 to 8.6 kDa resulted in high resolving power single-acquisition FT-ICR mass spectra with average charge-states highly correlated to those obtained by nanoESI, thus, providing strong evidence that the ESI process dictates the observed charge-state distribution. Importantly, unlike the recently introduced electrospray assisted laser desorption ionization (ELDI) source reported by Shiea and coworkers [1, 2], the data we have obtained to date rely on the use of an organic acid matrix. The results presented herein provide insight into the charging mechanism of this emerging ionization approach, while also expanding the utility of FT-ICR MS for top-down protein and complex mixture analysis.

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