GLYCOPATH INC — Department of Health and Human Services STTR Phase I: 300

Description

Increasinglyalterations in N linked glycans have been reported for serum or plasmaor for the most abundant serum glycoproteinimmunoglobulin Gfrom large cohorts of samples representing rheumatoid arthritisdigestive diseasescancer and liver fibrosisIn the case of fibrosistwo tests have identified alterations in Nlinked glycosylation on both total IgG populations and on specific IgG moleculesBoth of these tests can detect significant fibrosis with a high degree of accuracy and are also able to detect intermediate levels of fibrosisHoweverboth tests have drawbacks in that they require specialized sample handling resourcesextensive processing and purification prior to analysisand are expensive in regards to reagents and processingOur group has recently developed a streamlined antibody capture slide array approach to directly profile N glycans of captured serum glycoproteins like IgGa method requiring a few microliters of sample and simplified processing workflows that require no purification or sugar modifications prior to analysisThis parent method is referred to as the GlycoTyperIn this methodN linked glycans are released from antibody captured glycoproteins and are directly analyzed by MALDI TOF mass spectrometrysuch as the Bruker Tissuetyper MALDI TOFwhich is already available in clinical laboratoriesWe hypothesize that this method can be used to identify glycan biomarkers reflective of the changes that occur during the development of many diseasesincluding liver fibrosis cirrhosis as performed here NarrativeThis application will develop a new platform for glycan analysis and determine its ability to detect liver fibrosis