Mass Spectrometry used to be in the domain of Chemistry experts who spent a lot of their time on the floor pulling apart the instruments to make them work. The advent of Proteomics changed that and there are now amazing hardware and software developments which have allowed scientists to identify thousands of proteins in their systems and make valuable protein discoveries across diverse biologies.
What is less developed is the analysis of the modifications to these proteins – in my case particularly the glycosylation of these proteins which allows the ~10,000 human genes encoding for glycoproteins to have theoretically millions of glycoproteoforms. There is now a significant increase in glycosylation analysis in many research projects and international efforts initiated to integrate glycobiological knowledge1.
However, the total mammalian glycome is structurally complex and diverse and exists as many types of conjugates as well as those on proteins. The total mammalian glycome is composed of many glycan classes such as free oligosaccharides, glycosaminoglycans (GAGs), glycosphingolipids (GSLs), glycoproteins and other modified glycan features such as polysialic acids (PolySia), sulfation and proteoglycan attachments. To address this need for knowledge of the relationship between all the different components of a biological system, we have now extended our sequential release workflow2,3 for structural analysis of multiple conjugated glycan classes, including the subsequent improved proteomics analysis, from the same 10 ug sample, to move closer to enabling true multi-omics analyses to be achieved from the same sample.