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|Title: ||Enhanced analyte detection using in-source fragmentation of field asymmetric waveform ion mobility spectrometry-selected ions in combination with time-of-flight mass spectrometry|
|Authors: ||Brown, Lauren J.|
Smith, Robert W.
Toutoungi, Danielle E.
Reynolds, James C.
Bristow, Anthony W.T.
Wilson, Ian D.
Weston, Daniel J.
Creaser, Colin S.
|Issue Date: ||2012|
|Publisher: ||© American Chemical Society|
|Citation: ||BROWN, L.J. ... et al, 2012. Enhanced analyte detection using in-source fragmentation of field asymmetric waveform ion mobility spectrometry-selected ions in combination with time-of-flight mass spectrometry. Analytical Chemistry, 84 (9), pp. 4095 - 4103.|
|Abstract: ||Miniaturized ultra high field asymmetric waveform
ion mobility spectrometry (FAIMS) is used for the
selective transmission of differential mobility-selected ions
prior to in-source collision-induced dissociation (CID) and
time-of-flight mass spectrometry (TOFMS) analysis. The
FAIMS-in-source collision induced dissociation-TOFMS
(FISCID-MS) method requires only minor modification of
the ion source region of the mass spectrometer and is shown
to significantly enhance analyte detection in complex mixtures.
Improved mass measurement accuracy and simplified product
ion mass spectra were observed following FAIMS preselection and subsequent in-source CID of ions derived from
pharmaceutical excipients, sufficiently close in m/z (17.7 ppm mass difference) that they could not be resolved by TOFMS alone.
The FISCID-MS approach is also demonstrated for the qualitative and quantitative analysis of mixtures of peptides with FAIMS
used to filter out unrelated precursor ions thereby simplifying the resulting product ion mass spectra. Liquid chromatography
combined with FISCID-MS was applied to the analysis of coeluting model peptides and tryptic peptides derived from human
plasma proteins, allowing precursor ion selection and CID to yield product ion data suitable for peptide identification via
database searching. The potential of FISCID-MS for the quantitative determination of a model peptide spiked into human
plasma in the range of 0.45−9.0 μg/mL is demonstrated, showing good reproducibility (%RSD < 14.6%) and linearity (R2 >
|Description: ||This article is closed access.|
|Sponsor: ||The authors thank Loughborough University, Agilent Technologies,
and Owlstone Limited for financial support.|
|Publisher Link: ||http://dx.doi.org/10.1021/ac300212r|
|Appears in Collections:||Closed Access (Chemistry)|
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