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BU Mass Spec Resource to Collaborate With Bruker

NEW YORK (GenomeWeb News) – Bruker Daltonics and Boston University's Mass Spectrometry Resource plan to collaborate to apply high performance ion trap mass spectrometry and Fourier transform mass spec to glycomics and proteomics research, Bruker announced today.

Catherine Costello, director of the Boston University School of Medicine's Center for Biomedical Mass Spectrometry, and her colleagues plan to use Bruker's solariX FTMS with a 12 Tesla magnet, with electron transfer dissociation and electron capture dissociation capabilities, for their proteomics and glycomics studies.

Costello's laboratory, a National Institutes of Health-sponsored mass spec resource center, collaborates with other researchers to use mass spec for assessing biopolymers such as carbohydrates, lipids, and proteins. The team currently uses the Bruker amaZon ion trap mass spectrometer to analyze glycan structures in a detailed, high-throughput way and recently secured an NIH-NCRR High-End Shared Instrumentation Grant to obtain a solariX — a system that uses high mass resolving power and mass accuracy to discern complex mixtures of biopolymers.

The move is expected to augment the researchers' studies of complex carbohydrate structures and conjugates — polymers that are less structurally characterized than linear biopolymers such as proteins and oligonucleotides due to their branching and presence in mixtures. Using top-down and bottom-up proteomics approaches, Costello's team intends to employ FTMS for quickly uncovering the structure of biopolymers and post-translational modifications such as glycosylation.

Costello and her colleagues plan to develop workflows and high performance LC-FTMS/MS proteomics and glycomics approaches. In addition, Costello and Bruker plan to collaborate on developing methods for analyzing the structure of carbohydrates, such as a technique called "reverse" ETD — an approach in which negatively charged carbohydrate ions react with positively charged reagents to produce fragmentation.

"Bottom-up and top-down proteomics studies on the solariX FTMS will enhance our capabilities for the discovery of novel [post-translational modifications], including glycosylation," Costello said in a statement. "The availability of ETD, r-ETD, ECD, and multiple stages of CID MS/MS will greatly enhance our capabilities for the structural analysis of novel carbohydrate structures."

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