Invention novelty: a method for quantitative, high-throughput analysis of glycans from tissue sections
Value Proposition
Studies on protein glycosylation have been complicated by the diverse structure of protein glycans and the lack of effective tools to identify the protein glycosylation site and glycan structure. Currently, mass spectrometry is the major method for glycosylation analysis. Recently, mass spectrometry methods have been adapted for the analysis of protein markers, molecular diagnostics, infectious disease, and tissue analysis. However, tissue analysis for glycan modification of proteins are not currently available. This technology describes a method for quantitative analysis of glycans from tissue section via mass spectrometry imaging (MSI), which addresses unmet needs in the mass spectrometry market.
Advantages of this technology include:
§ Detailed structural information of the glycans
§ High mass resolution
§ Femtomole sensitivity of MS to detect low concentrations of molecules
§ Wide range of molecular weights detected by MSI
§ High-throughput analysis of tissue glycans
§ Quantitative
§ Capability of detecting unknown compound without any a priori knowledge
Technical Details
Johns Hopkins researchers have developed a method using mass spectrometry imaging (MSI) for direct profiling of N-linked glycans from fixed tissues. Mass spectrometry imaging (MSI) is a powerful tool that has been used to correlate various peptides, proteins, lipids and metabolites with their underlying histopathology in tissue sections. Features of this invention include: (1) direct profiling of glycans on tissues; (2) in situ chemical labeling and/or enzymatic modifications of glycans and glycoproteins on tissue slides; (3) quantitative analysis of tissue glycans and glycoproteins using isotopic labeling; and (4) targeted detection of glycans and proteins in situ by mass spectrometry. Commercial application of the technology includes direct imaging of glycans on tissues to determine biomarkers associated with disease-specific glycosylation changes.
Stage of Development: Pre-Clinical
Publication(s): WO 2013/177385
