TY - JOUR
T1 - TEMPO-Assisted Free Radical-Initiated Peptide Sequencing Mass Spectrometry (FRIPS MS) in Q-TOF and Orbitrap Mass Spectrometers
T2 - Single-Step Peptide Backbone Dissociations in Positive Ion Mode
AU - Jang, Inae
AU - Lee, Sun Young
AU - Hwangbo, Song
AU - Kang, Dukjin
AU - Lee, Hookeun
AU - Kim, Hugh I.
AU - Moon, Bongjin
AU - Oh, Han Bin
PY - 2017/1/1
Y1 - 2017/1/1
N2 - The present study demonstrates that one-step peptide backbone fragmentations can be achieved using the TEMPO [2-(2,2,6,6-tetramethyl piperidine-1-oxyl)]-assisted free radical-initiated peptide sequencing (FRIPS) mass spectrometry in a hybrid quadrupole time-of-flight (Q-TOF) mass spectrometer and a Q-Exactive Orbitrap instrument in positive ion mode, in contrast to two-step peptide fragmentation in an ion-trap mass spectrometer (reference Anal. Chem. 85, 7044–7051 (30)). In the hybrid Q-TOF and Q-Exactive instruments, higher collisional energies can be applied to the target peptides, compared with the low collisional energies applied by the ion-trap instrument. The higher energy deposition and the additional multiple collisions in the collision cell in both instruments appear to result in one-step peptide backbone dissociations in positive ion mode. This new finding clearly demonstrates that the TEMPO-assisted FRIPS approach is a very useful tool in peptide mass spectrometry research. [Figure not available: see fulltext.]
AB - The present study demonstrates that one-step peptide backbone fragmentations can be achieved using the TEMPO [2-(2,2,6,6-tetramethyl piperidine-1-oxyl)]-assisted free radical-initiated peptide sequencing (FRIPS) mass spectrometry in a hybrid quadrupole time-of-flight (Q-TOF) mass spectrometer and a Q-Exactive Orbitrap instrument in positive ion mode, in contrast to two-step peptide fragmentation in an ion-trap mass spectrometer (reference Anal. Chem. 85, 7044–7051 (30)). In the hybrid Q-TOF and Q-Exactive instruments, higher collisional energies can be applied to the target peptides, compared with the low collisional energies applied by the ion-trap instrument. The higher energy deposition and the additional multiple collisions in the collision cell in both instruments appear to result in one-step peptide backbone dissociations in positive ion mode. This new finding clearly demonstrates that the TEMPO-assisted FRIPS approach is a very useful tool in peptide mass spectrometry research. [Figure not available: see fulltext.]
KW - Free radical-initiated peptide sequencing (FRIPS)
KW - Orbitrap
KW - Q-TOF
KW - Radical-based fragmentations
KW - TEMPO
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U2 - 10.1007/s13361-016-1508-8
DO - 10.1007/s13361-016-1508-8
M3 - Article
C2 - 27686973
AN - SCOPUS:85006412429
VL - 28
SP - 154
EP - 163
JO - Journal of the American Society for Mass Spectrometry
JF - Journal of the American Society for Mass Spectrometry
SN - 1044-0305
IS - 1
ER -