SimGlycan®	What's new in this version

SimGlycan® predicts the structure of glycans and glycopeptides using mass spectrometry data. SimGlycan® accepts the experimental MS/MS data generated by a mass spectrometer, matches them with its own database of theoretical fragments and generates a list of probable candidate structures.

Each structure is scored to reflect how closely it matches your experimental data. Other biological information for the probable glycan structures such as the glycan class, reaction, pathway and enzyme are also made available for easy reference.

Glycan & Glycopeptide MS/MS Data Analysis Tool

SimGlycan® is an innovative glycan and glycopeptide MS/MS data analysis tool. SimGlycan® predicts the glycan structure, scores it and generates a list of probable glycans that closely match the experimental MS profile saving you hours of laborious glycan analysis work. For glycopeptide analysis, SimGlycan® identifies the peptides along with associated glycan structures, using the mass from enzymatically cleaved glycopeptides or precursor ion m/z values. MS/MS data analysis can be performed for a selected glycopeptide to check its proximity with the experimental data. No information regarding the peptide sequence or peptide mass is needed for this analysis.

SimGlycan® can identify complex glycosaminoglycan structures even when modified with substituents such as sulfate, phosphate, ethanolamine, etc. The spectra is annotated with subsequent loss of substituents from their corresponding glycosidic fragments. This functionality is useful for verifying the presence of carbohydrate residues modified with substituents.

Glycan & Glycopeptide MS/MS Data Analysis for Studying Glycosylation

Protein Glycosylation, which is a key post-translational modification, is the result of addition of a glycan to a peptide sequence. Glycopeptides are known to exhibit multiple biological functions. In order to identify distinct functional properties for defined structural features, detailed information on the respective glycan moieties is essential. In order to understand all these phenomena, glycosylation analysis is an area of growing interest. Glycans have also been found to participate in many biological processes including embryonic development, inter and intracellular activities, coordination of immune functions, pathogens homing on their host tissues, cell division processes and protein regulations and interactions.

Glycoprotein glycosylation analysis has since long been a challenging task for biochemists. SimGlycan® assists in predicting the structure of a glycan or glycopeptide from the MS/MS data acquired by mass spectrometry. It supports MS/MS profiles of both glycopeptides and released glycans with different chemical derivatives such as permethylation, and various reducing terminal modifications. These profiles can be uploaded in SimGlycan® using standard file formats or directly from mass spectrometer raw file formats from Applied Biosystems (AB Sciex TOF/TOF 5800, the AB SCIEX 4800 Plus MALDI TOF/TOF™ Analyzer, the AB SCIEX 4000 QTRAP® System, and the AB SCIEX QSTAR® Elite System) and Bruker Daltonics (ultrafleXtreme™ MALDI TOF/TOF, ultraflex™ MALDI TOF/TOF, autoflex™ TOF and TOF/TOF, maXis™ UHR-TOF, micrOTOF™, micrOTOF-Q™, solariX™ Qq-FTMS, and amaZon™ ion trap series).

SimGlycan® matches the experimental MS profiles with its own theoretical fragmentation database and generates a list of probable candidate glycan structures. Each structure is scored based on how closely it matches the experimental mass spectrometry data. Additional known biological information for the structures such as glycan class (N-Linked, O-Linked, heparin, lipopolysaccharide etc), reaction, pathway and enzyme is displayed, saving the time needed to retrieve this information from several resources. The predicted glycan structure along with its biological information facilitates glycosylation analysis, which in turn assists glycopeptide characterization.