Elucidating the sequence of intact bioactive peptides by using electron capture dissociation and hot electron capture dissociation in a linear radio-frequency quadrupole ion trap

Autor: Hiroyuki, Satake, Naomi, Manri, Akihito, Kaneko, Atsumu, Hirabayashi, Hideki, Hasegawa, Yuichiro, Hashimoto, Takashi, Baba, Takeshi, Sakamoto, Katsuyoshi, Masuda
Rok vydání: 2013
Předmět:
Zdroj: Rapid communications in mass spectrometry : RCM. 27(23)
ISSN: 1097-0231
3000-5000
Popis: Electron capture dissociation (ECD) is useful tool for sequencing of peptides and proteins with post-translational modifications. To increase the sequence coverage for peptides and proteins, it is important to develop ECD device with high fragmentation efficiency.Sequence analysis of intact undigested bioactive peptides (3000-5000 Da) was performed by use of electron capture dissociation (rf-ECD) and collision-induced dissociation (CID) in a linear radio-frequency quadrupole ion trap that was coupled to a time-of-flight mass spectrometer. We applied rf-ECD, hot rf-ECD (rf-ECD with high electron energy), and CID for intact bioactive peptide ions of various charge states and evaluated the sequence coverage of their fragment spectra.Hot rf-ECD produced a higher number of c- and z-type fragment ions of modified peptide ions as electron energy increased in lower charged peptide ions, and sequence coverage greater than 80% was obtained compared with the CID case (40-80%).The result indicates that intact bioactive modified peptides (Ghrelin, ANP) were correctly identified by use of hot rf-ECD.
Databáze: OpenAIRE
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