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Direct characterization of intact polypeptides by matrix‐assisted laser desorption electrospray ionization quadrupole Fourier transform ion cyclotron resonance mass spectrometry
Author(s) -
Sampson Jason S.,
Hawkridge Adam M.,
Muddiman David C.
Publication year - 2007
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/rcm.2947
Subject(s) - fourier transform ion cyclotron resonance , chemistry , mass spectrometry , electrospray ionization , analytical chemistry (journal) , ion cyclotron resonance , ionization , characterization (materials science) , quadrupole , fourier transform , ion , chromatography , atomic physics , cyclotron , optics , physics , organic chemistry , quantum mechanics
We report the characterization of a recently introduced hybrid ionization source, matrix‐assisted laser desorption electrospray ionization (MALDESI), coupled to a quadrupole Fourier transform ion cyclotron resonance mass spectrometry (QFT‐ICR‐MS) system. We first demonstrate the ability of MALDESI‐QFT‐ICR MS to directly analyze and provide high mass measurement accuracy (∼1 part‐per‐million) of a polypeptide using internal calibration. Second, we show the potential of MALDESI‐QFT‐ICR MS for the top‐down characterization of multiply charged polypeptide cations. Finally, we demonstrate sub‐femtomole detection limits in MALDESI‐QFT‐ICR MS using a combination of naturally occurring peptides and their respective stable isotope labeled forms. The results presented herein demonstrate the feasibility of several potential applications for MALDESI‐QFT‐ICR MS for the direct analysis of intact biological molecules. Copyright © 2007 John Wiley & Sons, Ltd.