AI Article Synopsis
- The study focuses on using thermal-assisted partial acid hydrolysis to break down carbohydrate parts of N-glycosylated peptides in horseradish peroxidase (HRP), aiming to create oligosaccharide cleavage ladders for mass spectrometry analysis.
- Different concentrations of trifluoroacetic acid were employed at various temperatures to selectively hydrolyze oligosaccharide units while minimizing peptide bond decomposition, and various glycopeptides of HRP were tested.
- Findings revealed that fucose is the most easily cleaved oligosaccharide, with specific glycopeptides carrying distinct oligosaccharide structures, helping in identifying glycopeptides and their monosaccharide compositions.
Article Abstract
Thermal-assisted partial acid hydrolysis of the carbohydrate moieties of N-glycosylated peptides of horseradish peroxidase (HRP) is used to generate oligosaccharide cleavage ladders. These ladders allow direct reading of components of the oligosaccharides by mass spectrometry. Acid hydrolysis performed with 1.4, 3.1, 4.5, or 6.7M trifluoroacetic acid at 37, 65, or 95 degrees C for 30min to 24h hydrolyzed mainly the oligosaccharide units of glycopeptides with least peptide bond or amino acid side chain hydrolysis. Tryptic N-glycosylated peptides from HRP with molecular weights of 2533, 2612, 3355, 3673, and 5647Da were used as test systems in these experiments. Data showed that the most labile group of oligosaccharides is the fucose (Fuc) and the majority of the end cleavage products are peptides with one or no N-acetylglucosamine (GlcNAc) residue linked to Asparagine (Asn). Additionally, the data agree with previous reports that glycopeptides 3355 and 3673Da carry an oligosaccharide (Xyl)Man3(Fuc)GlcNAc2, glycopeptide 5647Da carries two oligosaccharides (Xyl)Man3(Fuc)GlcNAc2, and glycopeptides 2612 and 2533Da carry (Xyl)Man3GlcNAc2 and (Fuc)GlcNAc, respectively. However, the glycosylation site of the 2612Da peptide at Asn286 is partially occupied. This method is particularly useful in identifying glycopeptides and obtaining monosaccharide compositions of glycopeptides.
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| http://dx.doi.org/10.1016/j.carres.2005.04.018 | DOI Listing |
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