Miniaturized Ultra High Field Asymmetric Waveform Ion Mobility Spectrometry Combined with Mass Spectrometry for Peptide Analysis
Autor: | James C. Reynolds, Lauren J. Brown, Danielle E. Toutoungi, Gushinder Kaur-Atwal, Neil A. Devenport, Colin S. Creaser, P. Boyle |
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Rok vydání: | 2010 |
Předmět: |
Ions
chemistry.chemical_classification Quantitative Biology::Biomolecules Electrospray Miniaturization Chromatography Protein mass spectrometry Ion-mobility spectrometry Molecular Sequence Data Analytical chemistry Peptide Bradykinin Mass spectrometry Tandem mass spectrometry Analytical Chemistry Ion chemistry Tandem Mass Spectrometry Trypsin Amino Acid Sequence Ion trap Peptides |
Zdroj: | Analytical Chemistry. 82:9827-9834 |
ISSN: | 1520-6882 0003-2700 |
DOI: | 10.1021/ac102125u |
Popis: | Miniaturized ultra high field asymmetric waveform ion mobility spectrometry (ultra-FAIMS) combined with mass spectrometry (MS) has been applied to the analysis of standard and tryptic peptides, derived from α-1-acid glycoprotein, using electrospray and nanoelectrospray ion sources. Singly and multiply charged peptide ions were separated in the gas phase using ultra-FAIMS and detected by ion trap and time-of-flight MS. The small compensation voltage (CV) window for the transmission of singly charged ions demonstrates the ability of ultra-FAIMS-MS to generate pseudo-peptide mass fingerprints that may be used to simplify spectra and identify proteins by database searching. Multiply charged ions required a higher CV for transmission, and ions with different amino acid sequences may be separated on the basis of their differential ion mobility. A partial separation of conformers was also observed for the doubly charged ion of bradykinin. Selection on the basis of charge state and differential mobility prior to tandem mass spectrometry facilitates peptide and protein identification by allowing precursor ions to be identified with greater selectivity, thus reducing spectral complexity and enhancing MS detection. |
Databáze: | OpenAIRE |
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