Boston University and Bruker Establish a Collaborative Effort in Glycomics and Advanced FTMS Applications
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Bruker Daltonics announced 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™ ion trap mass spectrometer for detailed and high throughput analyses of glycan structures, and have just ordered a solariX™ 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.
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™) 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 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 an ultra-high sensitivity implementation of ETD. The speed and sensitivity of the amaZon, together with fast MSn and ETD make it an ideal tool for obtaining in-depth structural information on complex carbohydrate structures.
The researchers at the Boston University School of Medicine are already using the recently introduced Bruker amaZon™ ion trap mass spectrometer for detailed and high throughput analyses of glycan structures, and have just ordered a solariX™ 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.
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™) 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 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 an ultra-high sensitivity implementation of ETD. The speed and sensitivity of the amaZon, together with fast MSn and ETD make it an ideal tool for obtaining in-depth structural information on complex carbohydrate structures.
