Boston University School of Medicine and Bruker Establish a Collaborative Effort in Glycomics and Advanced FTMS Applications.

BILLERICA, Mass. -- Bruker Daltonics announced today that it has established a collaboration with the Mass Spectrometry Resource laboratory of Professor Catherine Costello at the Boston University School of Medicine (BUSM). The collaborative effort will focus on the application of high performance ion trap mass spectrometry and Fourier Transform Mass Spectrometry (FTMS) to glycomics and proteomics applications. The researchers at the Boston University School of Medicine are already using the recently introduced Bruker amaZon(TM) ion trap mass spectrometer for detailed and high throughput analyses of glycan structures, and have just ordered a solariX(TM) FTMS with a 12 Tesla magnet for high performance bottom-up and top-down proteomics and glycomics with ETD and ECD capabilities.

Professor Costello is a Research Professor of Biochemistry, Biophysics and Chemistry, and the Director of the BUSM Center for Biomedical Mass Spectrometry. Her laboratory is a resource center sponsored by the NIH where mass spectrometry is applied to the study of biopolymers (proteins, carbohydrates and lipids) by local, national and international collaborators. The recent award of an NIH-NCRR High-End Shared Instrumentation Grant to the BUSM Center provided the funds for purchase of the solariX. Professor Costello and her group are recognized internationally as experts in the analysis of the complex structures of carbohydrates and their conjugates, such as glycoproteins and glycolipids. While these important classes of molecules are involved in immune system recognition, nervous system development, and many other critical biological processes, methods for their full structural characterization are less developed than for linear biopolymers such as proteins and oligonucleotides. Not only are the structures of carbohydrates more complex, because of their non-linear, branched structures, but they usually occur in complex mixtures.

The recently introduced Bruker solariX FTMS provides the highest mass resolving power and mass accuracy available on any mass spectrometer, making it ideally suited to tackle extremely complex mixtures. Additionally, the solariX offers the most versatile suite of tools for fragmenting biopolymers, including Collision Induced Dissociation (CID), either in the front-end collision cell and/or in the ICR cell, as well as Electron Capture Dissociation (ECD) in the ICR cell, and now even front-end Electron Transfer Dissociation (ETD). All of these structural tools are further augmented by the novel geometry of the solariX system that enables Continuous Accumulation of Selected Ions (CASI[TM]) for selectively enriching low abundant signals from specifically chosen carbohydrates, peptides or proteins.

The use of top-down and bottom-up proteomics techniques on the FTMS allows for rapid structural characterization of proteins and the discovery of Post-Translational Modifications (PTMs), including the glycosylation sites of particular interest to Professor Costello's group. Bruker Daltonics and Professor Costello's research group will work together to develop new workflows and approaches for high performance LC-FTMS/MS, using CID, ETD and ECD, for proteomics and glycomics research.

The Bruker amaZon ion trap offers unsurpassed ion trap speed and sensitivity including routine operation in MS3, up to 10 stages of MS/MS and a unique ultra-high sensitivity implementation of ETD. The speed and sensitivity of the amaZon, together with fast MS(n) and ETD make it an ideal tool for obtaining in-depth structural information on complex carbohydrate structures. Prof. Cathy Costello and Bruker Daltonics also plan to collaborate on the development of new methods for structural analysis of carbohydrates, such as the recently developed, "reverse" ETD (r-ETD), in which negatively charged carbohydrate ions with multiple charges are reacted with a positively charged reagent ion to induce fragmentation. This is an important development as ionization of carbohydrates is often much more efficient in negative ion mode, and the normal ETD process will not work with negative analyte ions.

Professor Cathy Costello commented: "We and our collaborators at the Boston University School of Medicine are already excited about the excellent results being obtained from the amaZon instrument. We now look forward to the delivery of the solariX FTMS system. Bottom-up and top-down proteomics studies on the solariX FTMS will enhance our capabilities for the discovery of novel PTMs, including glycosylation. 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."

"We are delighted that Professor Costello, who has an outstanding record in the development of mass spectrometry for new applications in the study of carbohydrates, has chosen Bruker as a partner in developing further applications of glycomics," stated Dr. Paul Speir, Bruker Daltonics' Vice President for FTMS. "We view our solariX ESI-FTMS with high field magnets as the ultimate platform for the characterization of complex mixtures and the structural analysis of the components of such mixtures. Further collaborative development of the amaZon as a high-throughput, high-performance research tool for the structural analysis of complex carbohydrates, and the collaboration on the optimization of both ETD and r-ETD methods for glycan analysis, make this a very exciting and important research collaboration for Bruker."

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