Distinguishing Core and Antenna Fucosylated Glycopeptides Based on Low-Energy Tandem Mass Spectra.
Anal Chem
; 90(21): 12776-12782, 2018 11 06.
Article
in En
| MEDLINE
| ID: mdl-30299079
ABSTRACT
A straightforward approach has been developed to distinguish core and antenna fucosylation in glycopeptides. The method does not require derivatization and can be easily adapted into a proteomics workflow. The key aspect is to use low collision energy collision-induced dissociation (CID) (on a quadrupole time-of-flight type instrument) when only single-step fragmentation processes occur. Low collision energy should show the precursor ion as the largest peak in the spectrum; the survival yield should be ideally over 50%, and this is obtained at a collision energy ca. 30% of that typically used for proteomics. In such a case, interfering processes like fucose migration or consecutive reactions are minimized. Core and antenna fucosylation can be discriminated using various ion abundance ratios. Low-energy CID spectra are very "clean" (no chemical noise), and the ions used for locating the fucose are among the major peaks, making the method well-suited for analytical work. Monitoring the change in the proportion of core and antenna fucosylation at the same glycosylation site is also feasible.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Orosomucoid
/
Glycopeptides
/
Prostate-Specific Antigen
/
Fucose
Limits:
Humans
Language:
En
Journal:
Anal Chem
Year:
2018
Type:
Article
Affiliation country:
Hungary