Glycosylation is a common post-translational modification (PTM) of proteins and plays a crucial role in many biological processes. Many disease biomarkers are glycosylated proteins.
Identification of intact glycopeptides based on mass spectrometry can provide information about the glycosite and attached glycan. However, the interpretation of acquired glycopeptide spectra remains difficult.
Recently, a research team led by Prof. YE Mingliang from the Dalian Institute of Chemical Physics (DICP) of the Chinese Academy of Sciences (CAS) developed a new glycoproteomics software tool, Glyco-Decipher, for the sensitive interpretation of the N-glycopeptide. high confidence mass spectra.
This study was published in Nature Communications on April 7.
The researchers found that the peptide backbone fragmentation pattern of glycopeptides was not affected by attached glycans or precursor charge states. And the high similarity of glycopeptide fragmentation pattern with identical peptide backbones was used to interpret the spectra of glycopeptides with low peptide fragmentation.
Additionally, the peptide identification scheme in Glyco-Decipher was independent of the glycan database, which allowed the discovery of unexpected glycans that were not present in the databases. Using the developed monosaccharide progression method, Glyco-Decipher was able to unveil unexpected glycans with modifying fragments in complex systems.
Additionally, the quantification module integrated into the software tool extracted the elution profiles of the glycopeptides, and thus enabled abundance analysis and functional studies of site-specific glycans.
“Glyco-Decipher is overall a very useful software tool for glycoproteomics,” commented one of the reviewers.
The study was supported by the National Key Research and Development Program of China, the National Natural Science Foundation of China and the CAS Youth Innovation Promotion Association.