Discrimination of GalNAc (4S/6S) sulfation sites in chondroitin sulfate disaccharides by chip-based nanoelectrospray multistage mass spectrometry

Sulfation pattern within chondroitin sulfate (CS) glycosaminoglycan (GAG) chains is an important post-translational modification that regulates their interaction with proteins. In this context, development of highly efficient and reproducible analytical methods for the investigation of CS sulfation...

Full description

Saved in:
Bibliographic Details
Published in:Central European journal of chemistry 2009-12, Vol.7 (4), p.752-759
Main Authors: Flangea, Corina, Serb, Alina F., Schiopu, Catalin, Tudor, Sorin, Sisu, Eugen, Seidler, Daniela G., Zamfir, Alina D.
Format: Article
Language:English
Subjects:
Biochemistry
Biological and Medical Physics
Biophysics
Chemistry
Chemistry and Materials Science
Chemistry/Food Science
Chondroitin sulfate
Fully automated chip-nanoESI
Geochemistry
High capacity ion trap mass spectrometry
Research Article
Sulfation sites
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Sulfation pattern within chondroitin sulfate (CS) glycosaminoglycan (GAG) chains is an important post-translational modification that regulates their interaction with proteins. In this context, development of highly efficient and reproducible analytical methods for the investigation of CS sulfation patterns is of high necessity. In this study we report a novel method for straightforward determination of N-acetylgalactosamine (GalNAc) sulfation sites in chondroitin sulfate disaccharides. Our protocol involves combining fully automated chip-based nanoelectrospray (nanoESI) for analyte infusion and ionization in negative ion mode with multistage (MS n ) collision-induced dissociation (CID) high capacity ion trap (HCT) mass spectrometry for generation of sequence ions diagnostic for identification of sulfate ester group position within GalNAc residues. The feasibility of this approach is here demonstrated on chondroitin 6-O-sulfate and chondroitin 4-O-sulfate disaccharides. Fragmentation patterns obtained by MS 2 and MS 3 sequencing stages provided first mass spectrometric data from which sulfation site(s) within GalNAc monosaccharide ring could be unequivocally deciphered. Hence, the method allowed discriminating 4S/6S sulfation sites solely on the basis of MS and multistage MS evidence.
ISSN:1895-1066
2391-5420
1644-3624
2391-5420
DOI:10.2478/s11532-009-0070-7