Wydział Chemii

Mateusz Waliczek

Remigiusz Bąchor

Monika Kijewska

Dorota Gąszczyk

Karolina Panek-Laszczyńska

Andrzej Konieczny

Krystyna Dąbrowska

Wojciech Witkiewicz

Karolina Marek-Bukowiec

Joanna Tracz

Magdalena Łuczak

Zbigniew Szewczuk

Piotr Stefanowicz

2019

Analytica Chimica Acta

1048

96-104

10.1016/j.aca.2018.10.012

Naukowa

Angielski

Artykuł

Enzymatic ¹⁸O exchange, the well-established approach in comparative proteomics, has some disadvantages such as back exchange of labeled oxygen and overlapping the peak of a labeled peptide with isotopic peaks of an unlabeled one. Herein we demonstrated a simple procedure in which samples digested with a trypsin (with and without H₂¹⁸O) were reacted with unlabeled and quadrupled ¹³C-labeled pyrylium salt respectively which results in formation of pyridinium cations. Thus, each isobarically labeled peptide containing zero or four ¹³C atoms in the mass reporter group, during tandem MS/MS forms an unique reporter ion useful for a relative quantitation. Such a sample treatment improves the signal to noise ratio, reduces overlapping of the isotopic peaks and completely eliminates the back exchange problem.

Isobaric labeling, Pyrylium salt, 18O, Ionization enhancers

http://dx.doi.org/10.1016/j.aca.2018.10.012

http://www.elsevier.com