Loading…
FeO@PANI: a magnetic polyaniline nanomaterial for highly efficient and handy enrichment of intact -glycopeptides
Glycosylation of proteins plays important roles in the occurrence and development of chronic diseases. In this study, we report an enrichment method of intact N -glycopeptides using a magnetic polyaniline nanomaterial (Fe 3 O 4 @PANI). Under the synergistic effect of hydrogen bonding and electrostat...
Saved in:
Published in: | Analyst (London) 2021-06, Vol.146 (13), p.4261-4267 |
---|---|
Main Authors: | , , , , , , , , |
Format: | Article |
Language: | |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Summary: | Glycosylation of proteins plays important roles in the occurrence and development of chronic diseases. In this study, we report an enrichment method of intact
N
-glycopeptides using a magnetic polyaniline nanomaterial (Fe
3
O
4
@PANI). Under the synergistic effect of hydrogen bonding and electrostatic adsorption, Fe
3
O
4
@PANI can rapidly and easily enrich
N
-glycopeptides derived from standard protein (bovine fetuin and transferrin) tryptic digests and serum haptoglobin tryptic digests. Finally we have detected 63 glycopeptides in the glycosylation sites of both N204 and N211 from the serum haptoglobin beta chain using MALDI FTICR MS. Compared with non-magnetic materials, Fe
3
O
4
@PANI can achieve complete separation from complex biological samples, meeting the requirement of the high purity of samples for mass spectrometric detection. Overall, Fe
3
O
4
@PANI exhibits great application potential in the highly efficient enrichment of intact
N
-glycopeptides due to its stability and convenient preparation.
Fe
3
O
4
@PANI can be utilized in efficiently enriching intact
N
-glycopeptides from complex biological samples based on hydrogen bond and electrostatic adsorption between glycopeptides and this bifunctional nanomaterial. |
---|---|
ISSN: | 0003-2654 1364-5528 |
DOI: | 10.1039/d1an00580d |